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Overexpression of integral membrane proteins for structural studies

Published online by Cambridge University Press:  17 March 2009

R. Grisshammer  and
C. G. Tateu
R. Grisshammer
Affiliation:
Centre for Protein Engineering
C. G. Tateu
Affiliation:
Laboratory of Molecular Biology, MRC Centre, Hills Road, CambridgeCB2 2QH, UK
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Extract

Determination of the structure of integral membrane proteins is a challenging task that is essential to understand how fundamental biological processes (such as photosynthesis, respiration and solute translocation) function at the atomic level. Crystallisation of membrane proteins in 3D has led to the determination of four atomic resolution structures [photosynthetic reaction centres (Allen et al. 1987; Chang et al. 1991; Deisenhofer & Michel, 1989; Ermler et al. 1994); porins (Cowan et al. 1992; Schirmer et al. 1995; Weiss et al. 1991); prostaglandin H2 synthase (Picot et al. 1994); light harvesting complex (McDermott et al. 1995)], and crystals of membrane proteins formed in the plane of the lipid bilayer (2D crystals) have produced two more structures [bacteriorhodopsin (Henderson et al. 1990); light harvesting complex (Kühlbrandt et al. 1994)].

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 28 , Issue 3 , August 1995 , pp. 315 - 422
Copyright
Copyright © Cambridge University Press 1995

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References

Aeed, P. A. & Elhammer, A. P. (1994). Glycosylation of prorenin in insect cells: the insect cell line Sf9 does not express the mannose 6–phosphate recognition signal. Biochemistry 33, 8793–8797.CrossRefGoogle Scholar
Aharony, D., Little, J., Powell, S., Hopkins, B., Bundell, K. R.McPheat, W. L.Gordon, R. D.Hassal, G., Hockney, R., Griffen, R. & Graham, A. (1993). Pharmacological characterisation of cloned human NK-2 (Neurokinin A) receptor expressed in a baculovirus/Sf21 insect cell system. Mol. Pharmacol. 44, 356–363.Google Scholar
Alexander, W. A., Moss, B. & Fuerst, T. R. (1992). Regulated expression of foreign genes in Vaccinia virus under the control of bacteriophage T7 RNA polymerase and the Escherichia coli lac repressor. J. Virology 66, 2934–2942.CrossRefGoogle ScholarPubMed
Allen, J. P., Feher, G., Yeates, T. O., Komiya, H. & Rees, D. C. (1987). Structure of the reaction center from Rhodobacter sphaeroides R-26: The cofactors. Proc. Natl. Acad. Sci. USA 84, 5730–5734.CrossRefGoogle ScholarPubMed
Altmann, F., Kornfeld, G., Dalik, T., Staudacher, E. & Glossl, J. (1993). Processing of asparagine-linked oligosaccharides in insect cells. N-Acetylgluco-saminyltransferase I and II activities in cultured lepidopteran cells. Glycobiology 3, 619–625.CrossRefGoogle Scholar
Amorim, A. G., CARDOSO-De-Almeida, M. L., Carrington, M., Morga, D. P., Riezman, H., Zerbini, L. F., Piestun, V. S. & Castilho-ValaviciuS, B. A. (1994). Expression of Mycobacterium leprae 18-kDa antigen in yeast in a GPI-anchored form. Brazilian J. Med. Biol. Res. 27, 623–626.Google Scholar
Anderson, J. A., Huprikar, S. S., Kochian, L. V., LUCAS, W. J. & Gaber, R. F. (1992). Functional expression of a probable Arabidopsis thaliana potassium channel in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 89, 3736–3740.CrossRefGoogle ScholarPubMed
Aoyama, T., Korzekwa, K., Nagata, K., Gillette, J., Gelboin, H. V. & Gonzales, F. J. (1989 a). cDNA-directed expression of rat testosterone 7α-hydroxylase using the modified Vaccinia virus, T7-RNA-polymerase system and evidence for 6α-hydroxylation and Δ6-testosterone formation. Eur. J. Biochem. 181, 331–336.CrossRefGoogle Scholar
Aoyama, T., Yamano, S., Waxman, D. J., Lapenson, D. P., Meyer, U. A., Fischer, V., Tyndale, R., Inaba, T., Kalow, W., Gelboin, H. V. & Gonzales, F. J. (1989 b). Cytochrome P-450 hPCN3, a novel cytochrome P-450 IIIA gene product that is differentially expressed in adult human liver. J. Biol. Chem. 264, 10388–10395.CrossRefGoogle ScholarPubMed
Arffman, A., Aho, S., Torkkeli, H. & Korhola, M. (1990). Isolation and characterisation of yeast mutants supersecreting Trichoderma reesii endoglucanase I (EGI). Yeast 6, S438.Google Scholar
Asano, T., Katagir, H., Takata, K., Lin, J.-L., Ishihara, H., Inukai, K., Tsukuda, K., Kikuchi, M., Hirano, H., Yazaki, Y. & Oka, Y. (1991). The role of Nglycosylation of GLUT1 for glucose transport activity. J. Biol. Chem. 266, 24632–24636.CrossRefGoogle ScholarPubMed
Asseffa, A., Smith, S. J., Nagata, K., Gillette, J., Gelboin, H. V. & Gonzalez, F. J. (1989). Novel exogenous heme-dependent expression of mammalian cytochrome P450 using baculovirus. Arch. Biochem. Biophys. 274, 481–490.CrossRefGoogle ScholarPubMed
Atwater, J. A., Wisdom, R. & Verma, I. M. (1990). Regulated mRNA stability. Annu. Rev. Genet. 24, 519–541.CrossRefGoogle ScholarPubMed
Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. & Struhl, K. (1994). Current protocols in molecular biology. New York: Greene Publishing Associates and Wiley-Interscience, John Wiley & Sons.Google Scholar
Baker, E. K., Colley, N. J. & Zuker, C. S. (1994). The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J. 13, 4886–4895.CrossRefGoogle ScholarPubMed
Baldwin, S. A., Baldwin, J. M., Gorga, F. R. & Lienhard, G. E. (1979). Purification of the cytochalasin B binding component of the human erythrocyte monosaccharide transport system. Biochim. Biophys. Ada 552, 183–188.CrossRefGoogle ScholarPubMed
Bardwell, J. C. A., Lee, J. O., Jander, G., Martin, N., Belin, D. & Beckwith, J. (1993). A pathway for disulfide bond formation in vivo. Proc. Natl. Acad. Sci. USA 90, 1038–1042.CrossRefGoogle ScholarPubMed
Bardwell, J. C. A., McGovern, K. & Beckwith, J. (1991). Identification of a protein required for disulfide bond formation in vivo. Cell 67, 581–589.CrossRefGoogle ScholarPubMed
Barnes, H. J., Arlotto, M. P. & Waterman, M. R. (1991). Expression and enzymatic activity of recombinant cytochrome P450 17α-hydroxylase in Escherichia coli. Proc. Natl. Acad. Sci. USA 88, 5597–5601.CrossRefGoogle Scholar
Barnett, J., Chow, J., Ives, D., Chiou, M., Mackenzie, R., Osen, E., Nguyen, B., Tsing, S., Bach, C., Freire, J., Chan, H., Sigal, E. & Ramesha, C. (1994). Purification, characterization and selective inhibition of human prostaglandin G/H synthase 1 and 2 expressed in the baculovirus system. Biochim. Biophys. Acta 1209, 13O–139.CrossRefGoogle ScholarPubMed
Belsham, G. J., Barker, D. G. & Smith, A. E. (1986). Expression of polyoma virus middle-T antigen in Saccharomyces cerevisiae. Eur. J. Biochem. 156, 413–421.CrossRefGoogle ScholarPubMed
Belyaev, A. S. & Roy, P. (1993). Development of baculovirus triple and quadruple expression vectors: co-expression of three or four bluetongue virus proteins and the synthesis of bluetongue virus-like particles in insect cells. Nucleic Acids Res. 21, 1219–1223.CrossRefGoogle ScholarPubMed
Bergeron, J. J. M., Brenner, M. B., Thomas, D. Y. & Williams, D. B. (1994). Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. Trends Biochem. Sci. 19, 124–128.CrossRefGoogle ScholarPubMed
Berglund, P., Ströberg, M., Garoff, H., Atkins, G. J., Sheahan, B. J. & Liljeström, P. (1993). Semliki Forest virus expression system: production of conditionally infectious recombinant particles. Bio/Technology 11, 916–920.Google ScholarPubMed
Bertin, B., Freissmuth, M., Breyer, R. M., Schütz, W., Strosberg, A. D. & Marullo, S. (1992). Functional expression of the human serotonin 5-HT1A receptor in Escherichia coli. J. Biol. Chem. 267, 8200–8206.CrossRefGoogle ScholarPubMed
Bibi, E., Gros, P. & Kaback, H. R. (1993). Functional expression of mouse mdri in Escherichia coli. Proc. Natl. Acad. Sci. USA 90, 9209–9213.CrossRefGoogle Scholar
Bilous, P. T. & Weiner, J. H. (1988). Molecular cloning and expression of the Escherichia coli dimethyl sulfoxide reductase operon. J. Bacteriol. 170, 1511–1518.CrossRefGoogle ScholarPubMed
Bishop, D. H. L. (1994). Baculovirus-based expression systems. In Membrane Protein Expression Systems. A User's Guide, (ed. Gould, G. W.), pp. 83–124. London: Portland Press.Google Scholar
Bissinger, P. H. & Kuchler, K. (1994). Molecular cloning and expression of the Saccharomyces cerevisiae STS1 gene product. J. Biol. Chem. 269, 4180–4186.CrossRefGoogle ScholarPubMed
Blachly-Dyson, E., Zambronicz, E. B., Yu, W. H., Adams, V., McCabe, E. R. B., Adelman, J., Colombini, M. & Forte, M. (1993). Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage dependent anion channel. J. Biol. Chem. 268, 1835–1841.CrossRefGoogle ScholarPubMed
Blakely, R. D., Clark, J. A., Rudnick, G. & Amara, S. G. (1991). Vaccinia-T7 RNA polymerase expression system: evaluation for the expression cloning of plasma membrane transporter. Anal. Biochem. 194, 302–308.CrossRefGoogle Scholar
Blanco, G., Xie, Z. J. & Mercer, R. W. (1993). Functional expression of the α2 and α3 isoforms of the Na, K-ATPase in baculovirus infected cells. Proc. Natl. Acad. Sci. USA 90, 1824–1828.CrossRefGoogle Scholar
Blount, P. & Merlie, J. P. (1991). BiP associates with newly synthesized subunits of the mouse muscle nicotinic receptor. J. Cell Biol. 113, 1125–1132.CrossRefGoogle ScholarPubMed
Blumer, K. J., Reneke, J. E. & Thorner, J. (1988). The STE2 gene product is the ligand-binding component of the α-factor receptor of Saccharomyces cerevisiae J. Biol. Chem. 263, 10836–10842.CrossRefGoogle ScholarPubMed
Blusch, J., Morandini, P. & Nellen, W. (1992). Transcriptional regulation by folate: inducible gene expression in Dictyostelium transformants during growth and early development. Nucleic Acids Res. 20, 6235–6238.CrossRefGoogle ScholarPubMed
Bonning, B. C., Roelvink, P. W., Vlak, J. M., Possee, R. D. & Hammock, B. D. (1994). Superior expression of juvenile hormone esterase and β-galactosidase from the basic protein promoter of Autographa californica nuclear polyhedrosis virus compared to the pio and polyhedrin promoter. J. Gen. Virol. 75, 1551–1556.CrossRefGoogle Scholar
Braell, W. A. & Lodisch, H. F. (1982). The erythrocyte anion transport protein is cotranslationally inserted into microsomes. Cell 28, 23–31.CrossRefGoogle Scholar
Braiman, M. S., Stern, L. J., Chao, B. H. & Khorana, H. G. (1987). Structure-function studies on bacteriorhodopsin-IV. Purification and renaturation of bacterio-opsin polypeptide expressed in Escherichia coli. J. Biol. Chem. 262, 9271–9276.CrossRefGoogle ScholarPubMed
Bravo, D. A., Gleason, J. B., Sanchez, R. I., Roth, R. A. & Fuller, R. S. (1994). Accurate and efficient cleavage of the human insulin proreceptor by the human proprotein-processing protease furin. J. Biol. Chem. 269, 25830–25837.CrossRefGoogle ScholarPubMed
Bresnahan, M. R., Flordellis, C. S., Vassilatis, D. K., Makrides, S. C.Zannis, V. I. & Gavras, H. (1990). High level of expression of functional human platelet α2- adrenergic receptors in a stable mouse C127 cell line. Biochim. Biophys. Acta 1052, 439–445.CrossRefGoogle Scholar
Breyer, R. M., Strosberg, A. D. & Guillet, J.-G. (1990). Mutational analysis of ligand binding activity of β2-adrenergic receptor expressed in Escherichia coli. EMBO J. 9, 2679–2684.CrossRefGoogle Scholar
Brian, W. R., Sari, M.-A., Iwasaki, M., Shimada, T., Kaminsky, L. S. & Guengerich, F. P. (1990). Catalytic activities of human liver cytochrome P-450 IIIA4 expressed in Saccharomyces cerevisiae. Biochemistry 29, 11280–11292.CrossRefGoogle ScholarPubMed
Broome-Smith, J. K., Tadayyon, M. & Zhang, Y. (1990). β-lactamase as a probe of membrane protein assembly and protein export. Molec. Microbiol. 4, 1637–1644.CrossRefGoogle ScholarPubMed
Buters, J. T. M., Korzekwa, K. R., Kunze, K. L., Omata, Y., Hardwick, J. P. & Gonzalez, F. J. (1994). cDNA-directed expression of human cytochrome P450 CYP3A4 using baculovirus. Drug Metabolism Disposition 22, 688–692.Google ScholarPubMed
Cahoreau, C., Garnier, L., Djiane, J., Devauchelle, G. & Cerutti, M. (1994). Evidence for N-glycosylation and ubiquitination of the prolactin receptor expressed in a baculovirus-insect cell system. FEBS Lett. 350, 230–234.CrossRefGoogle Scholar
Cahoreau, C., Petridou, B., Cerutti, M., Djiane, J. & Devauchelle, G. (1992). Expression of the full-length rabbit prolactin receptor and its specific domains in baculovirus infected insect cells. Biochimie 74, 1053–1065.CrossRefGoogle ScholarPubMed
Cammarata, K. V. & Schmidt, G. W. (1992). In vitro reconstitution of a lightharvesting gene product: Deletion mutagenesis and analysis of pigment binding. Biochemistry 31, 2779–2789.CrossRefGoogle Scholar
Carter, D. B., Thomsen, D. R., IM, W. B., Lennon, D. J., Ngo, D. M., Gale, W., Im, H. K., Seeburg, P. H. & Smith, M. W. (1992). Functional expression of GABA-A chloride channels and benzodiazepine binding sites in baculovirus infected insect cells. Bio/Technology 10, 679–681.Google ScholarPubMed
Cascio, M., Schoppa, N. E., Grodzicki, R. L., Sigworth, F. J. & Fox, R. O. (1993). Functional expression and purification of a homomeric human α1 glycine receptor in baculovirus-infected insect cells. J. Biol. Chem. 268, 22135–22142.CrossRefGoogle Scholar
Centeno, F., Deschamps, S., Lompre, A.-M., Anger, M., Moutin, M.-J., Dupont, Y., Palmgren, M. G., Villalba, J. M., Moller, J. V., Falson, P. & Le Maire, M. (1994). Expression of the sarcoplasmic reticulum Ca2+-ATPase in yeast. FEBS Lett. 354, 117–122.CrossRefGoogle ScholarPubMed
Chang, C.-H., El-Kabbani, O., Tiede, D., Norris, J. & Schiffer, M. (1991). Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry 30, 5352–5360.CrossRefGoogle ScholarPubMed
Changeux, J.-P., Kasai, M. & Lee, C.-Y. (1970). Use of a snake venom toxin to characterize the cholinergic receptor protein. Proc. Natl. Acad. Sci. USA 67, 1241–1247.CrossRefGoogle ScholarPubMed
Chaudhri, M., Steverding, D., Kittelberger, D., Tjia, S. & Overath, P. (1994). Expression of a GPI-anchored Trypanosoma brucei transferring-binding protein complex in insect cells. Proc. Natl. Acad. Sci. USA 91, 6443–6447.CrossRefGoogle Scholar
Chirino, A. J., Lous, E. J., Huber, M., Allen, J. P., Schenck, C. C., Paddock, M. L., Feher, G. & Rees, D. C. (1994). Crystallographic analyses of site–directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry 33, 4584–4593.CrossRefGoogle ScholarPubMed
Chisholm, V., Chen, C. Y., Simpson, N. J. & Hitzeman, R. J. (1990). Molecular and genetic approach to enhancing protein secretion. Methods Enzymol. 185, 471–482.CrossRefGoogle ScholarPubMed
Christophe, P. R., Robert, P., Maugain, S., Bellet, D., Koman, A. & Bidart, J.-H. (1993). Expression of the human follicle stimulating hormone receptor in the baculovirus system. Biochem. Biophys. Res. Commun. 196, 402–408.CrossRefGoogle ScholarPubMed
Cline, S. W. & Doolittle, W. F. (1987). Efficient transfection of the archaebacterium Halobacterium halobium. J. Bacteriol. 169, 1341–1344.CrossRefGoogle ScholarPubMed
Cline, S. W., Schalkwyk, L. C. & Doolittle, W. F. (1989). Transformation of the archaebacterium Halobacterium volcanii with genomic DNA. J. Bacteriol. 171, 4987–4991.CrossRefGoogle ScholarPubMed
Colville, C. A. & Gould, G. W. (1994). Expression of membrane transport proteins in Xenopus oocytes. In Membrane protein expression systems. A user's guide, (ed. Gould, G. W.), pp. 243–274. London: Portland Press.Google Scholar
Connerton, I. F. (1994). Expression of membrane proteins in yeast. In Membrane protein expression systems. A user's guide, (ed. Gould, G. W.), pp. 177–218. London: Portland Press.Google Scholar
Consler, T. G., Persson, B. L., Jung, H., Zen, K. H., Jung, K., Privé, G. G., Verner, G. E. & Kaback, H. R. (1993). Properties and purification of an active biotinylated lactose permease from Escherichia coli. Proc. Natl. Acad. Sci. USA 90, 6934–6938.CrossRefGoogle ScholarPubMed
Cope, D. L., Holman, G. D., Baldwin, S. A. & Wolstenholme, A. J. (1994). Domain assembly of the GLUT1 glucose transporter. Biochem. J. 300, 291–294.CrossRefGoogle ScholarPubMed
Couturier, S., Bertrand, D., Matter, J.-M., Hernandez, M.-C., Bertrand, S., Millar, N., Valera, S., Barkas, T. & Ballivet, M. (1990). A neuronal nicotinic acetylcholine receptor subunit (α7) is developmentally regulated and forms a homooligomeric channel blocked by a-BTX. Neuron 5, 847–856.CrossRefGoogle Scholar
Cowan, S. W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R. A., Jansonius, J. N. & Rosenbusch, J. P. (1992). Crystal structures explain functional properties of two E. coli porins. Nature 358, 727–733.CrossRefGoogle ScholarPubMed
Crespi, C. L., Penman, B. W., Steimel, D. T., Gelboin, H. V. & Gonzales, F. J. (1991). The development of a human cell line stably expressing human CYP3A4: role in the metabolic activation of aflatoxin B1 and comparison to CYP1A2 and CYP2A3. Carcinogenesis 12, 355–359.CrossRefGoogle ScholarPubMed
Cromlish, W. A., Payette, P., Culp, S. A., Ouellet, M., Percival, M. D. & Kennedy, B. P. (1994). High-level expression of active human cyclooxygenase-2 in insect cells. Arch. Biochem. Biophys. 314, 193–199.CrossRefGoogle ScholarPubMed
Danbolt, N. C., Pines, G. & Kanner, B. I. (1990). Purification and reconstitution of the sodium-and potassium-coupled glutamate transport glycoprotein from rat brain. Biochemistry 29, 6734–6740.CrossRefGoogle ScholarPubMed
Davidson, D. J. & Castellino, F. J. (1991). Asparagine-linked oligosaccharide processing in lepidopteran insect cells. Temporal dependence of the nature of the oligosaccharides assembled on asparagine-289 of recombinant human plasminogen produced in baculovirus vector infected Spodoptera frugiperda (IPLB-SF-21AE) cells. Biochemistry 30, 6167–6174.CrossRefGoogle ScholarPubMed
Davies, A. & Morgan, B. P. (1993). Expression of the GPI-linked complementinhibiting protein CD59 antigen in insect cells using a baculovirus vector. Biochem. J. 295. 889–896.CrossRefGoogle ScholarPubMed
Davies, A. H., Jowett, J. B. M. & Jones, I. M. (1993). Recombinant baculovirus vectors expressing glutathione-S-transferase fusion proteins. Bio/Technology 11, 933–936.Google ScholarPubMed
Davis, T. R., Shuler, M. L., Granados, R. R. & Wood, H. A. (1993 a). Comparison of oligosaccharide processing among various insect cell lines expressing a secreted glycoprotein. In Vitro Cell. Dev. Biol. 29A, 842–846.CrossRefGoogle ScholarPubMed
Davis, T. R., Wickham, T. J., McKenna, K. A., Granados, R. R., Shuler, M. L. & Wood, H. A. (1993 b). Comparative recombinant protein production of eight insect cell lines. In Vitro Cell. Dev. Biol. 29A, 388–390.CrossRefGoogle ScholarPubMed
Deisenhofer, J. & Michel, H. (1989). The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis. EMBO J. 8, 2149–2170.CrossRefGoogle ScholarPubMed
Detomaso, A. W., Xie, Z. J., Liu, G. & Mercer, R. W. (1993). Expression, targeting and assembly of functional Na, K-ATPase polypeptides in baculovirus-infected insect cells. J. Biol. Chem. 268, 1470–1478.CrossRefGoogle ScholarPubMed
Dierstein, R. & Gad'on, N. (1993). Expression study with the Escherichia colt lep gene for leader peptidase in phototrophic purple bacteria. Arch. Microbiol. 159, 101–108.CrossRefGoogle Scholar
Dobberstein, B. (1994). Protein transport-On the beaten pathway. Nature 367, 599–600.CrossRefGoogle ScholarPubMed
Domingo, D. L. & Trowbridge, I. S. (1988). Characterisation of the human transferrin receptor produced in a baculovirus expression system. J. Biol. Chem. 263, 13386–13392.CrossRefGoogle Scholar
Dornmair, K., Kiefer, H. & Jahnig, F. (1990). Refolding of an integral membrane protein. J. Biol. Chem. 265, 18907–18911.CrossRefGoogle ScholarPubMed
Dou, D., Owolabi, J. B., Dey, S. & Rosen, B. P. (1992). Construction of a chimeric ArsA-ArsB protein for overexpression of the oxyanion-translocating ATPase. J. Biol. Chem. 267, 25768–25775.CrossRefGoogle ScholarPubMed
Dubendorff, J. W. & Studier, F. W. (1991). Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressor. J. Mol. Biol. 219, 45–59.CrossRefGoogle Scholar
Dunn, R. J., Hackett, N. R., McCoy, J. M., Chao, B. H., Kimura, K. & Khorana, H. G. (1987). Structure-function studies on bacteriorhodopsin – I. Expression of the bacterio-opsin gene in Escherichia coli. J. Biol. Chem. 262, 9246–9254.CrossRefGoogle ScholarPubMed
Eakle, K. A., Kim, K. S., Kabalin, M. A. & Farley, R. A. (1992). High-affinity ouabain binding by yeast cell expressing Na+, K+-ATPase α subunits and the gastric H+, K+ATPase β subunit. Proc. Natl. Acad. Sci. USA 89, 2834–2838.CrossRefGoogle ScholarPubMed
Earl, P. L., Moss, B. & Doms, R. W. (1991). Folding, interaction with GRP78-B1P, assembly, and transport of the human immunodeficiency virus type 1 envelope protein., J. Virol. 65, 2047–2055.CrossRefGoogle Scholar
Eckert, B. & Beck, C. F. (1989). Overproduction of transposon Tn10-encoded tetracycline resistance protein results in cell death and loss of membrane potential. J. Bacteriol. 171, 3557–3559.CrossRefGoogle ScholarPubMed
Efimov, V. A., Fradkov, A. F., Raskind, A. B., Khristin, M. S., Klimov, V. V. & Chakhmakhcheva, O. G. (1994). Expression of the barley psbA gene in Escherichia coli yields a functional in vitro photosystem II protein Di. FEBS Lett. 348, 153–157.CrossRefGoogle Scholar
Eidne, K. A. (1994). Expression of receptors in Xenopus oocytes. In Membrane protein expression systems. A user's guide, (ed. Gould, G. W.), pp. 275–300. London: Portland Press.Google Scholar
Eistetter, H. R., Church, D. J., Mills, A., Godfrey, P. P., Capponi, A. M., Brewster, R., Schulz, M.-F., Kawashima, E. & Arkinstall, S. J. (1991). Recombinant bovine neurokinin-2 receptor stably expressed in Chinese hamster ovary cells couples to multiple signal transduction pathways. Cell Regulation 2, 767–779.CrossRefGoogle ScholarPubMed
Ellis, L., Clauser, E., Morgan, D. O., Edery, M., Roth, R. A. & Rutter, W. J. (1986). Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell 45, 721–732.CrossRefGoogle ScholarPubMed
Ellis, R. J. & Van Der Vies, S. M. (1991). Molecular chaperones. Annu. Rev. Biochem. 60, 321–347.CrossRefGoogle ScholarPubMed
Ermler, U., Fritzsch, G., Buchanan, S. K. & Michel, H. (1994). Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2·65 Å resolution: cofactors and protein-cofactor interactions. Structure 2, 925–936.CrossRefGoogle ScholarPubMed
Erni, B. & Zanolari, B. (1986). Glucose-permease of the bacterial phosphotransferase system. J. Biol. Chem. 261, 16398–16403.CrossRefGoogle Scholar
Fafournoux, P., Ghysdael, J., Sardet, C. & Pouyssegur, J. (1991). Functional expression of the human growth factor activatable Na+/H+ Antiporter (NHE-1) in baculovirus-infected cells. Biochemistry 30, 9510–9515.CrossRefGoogle ScholarPubMed
Falck-Pedersen, E., Heinflink, M., Alvira, M., Nussenzveig, D. R. & Gershengorn, M. C. (1994). Expression of thyrotropin-releasing hormone receptors by adenovirusmediated gene transfer reveals that thyrotropin-releasing hormone desensitization is cell specific. Molec. Pharmacol. 45, 684–689.Google ScholarPubMed
Farchaus, J. W. & Oesterhelt, D. (1989). A Rhodobacter sphaeroides puf L, M and X deletion mutant and its complementation in trans with a 5–3 kb puf operon shuttle fragment. EMBO J.. 8, 47–54.CrossRefGoogle Scholar
Felder, C. C., Veluz, J. S., Williams, H. L., Briley, E. M. & Matsuda, L. A. (1992). Cannabinoid agonists stimulate both receptor- and non-receptor-mediated signal transduction pathways in cells transfected with and expressing cannabinoid receptor clones. Molec. Pharmacol. 42, 838–845.Google ScholarPubMed
Ferrandomay, E., Brustmann, B. & Oesterhelt, D. (1993). A C–terminal truncation results in high-level expression of the functional photoreceptor sensory rhodopsin-I in the archaeon Halobacterium salinarium. Molec. Microbiol. 9, 943–953.CrossRefGoogle ScholarPubMed
Ferreira, G. C. & Pedersen, P. L. (1992). Overexpression of higher eukaryotic membrane proteins in bacteria - Novel insights obtained with the liver mitochondrial proton/phosphate symporter. J. Biol. Chem. 267, 5460–5466.CrossRefGoogle ScholarPubMed
Ferrer, A., Aparicio, C., Nogues, N., Wettstein, A., Bach, T. J. & Boronat, A. (1990). Expression of catalytically active radish 3-hydroxy-3-methylglutaryl coenzyme A reductase in Escherichia coli. FEBS Lett. 266, 67–71.CrossRefGoogle Scholar
Fiermonte, G., Walker, J. E. & Palmieri, F. (1993). Abundant bacterial expression and reconstitution of an intrinsic membrane-transport protein from bovine mitochondria. Biochem. J. 294, 293–299.CrossRefGoogle ScholarPubMed
Findlay, J. B. C. (1990 a). Purification of membrane proteins. In Protein purification applications. A practical approach, (ed. Harris, E. L. V. & Angal, S.), pp. 59–82. Oxford, UK: Oxford University Press.Google Scholar
Findlay, J. B. C. (1990 b). Purification of proteins for sequencing. In Protein purification applications. A practical approach, (ed. Harris, E. L. V. & Angal, S.), pp. 83–90. Oxford, UK: Oxford University Press.Google Scholar
Ford, C. F., Suominen, I. & Glatz, C. E. (1991). Fusion tails for the recovery and purification of recombinant proteins. Protein Express. Purific. 2, 95–107.CrossRefGoogle ScholarPubMed
Fornari, C. S. & Kaplan, S. (1982). Genetic transformation of Rhodopseudomonas sphaeroides by plasmid DNA. J. Bacterial. 152, 89–97.CrossRefGoogle ScholarPubMed
Fraser, C. M., Arakawa, S., McCombie, W. R. & Venter, J. C. (1989). Cloning, sequence analysis, and permanent expression of a human α2-adrenergic receptor in Chinese Hamster Ovary cells, J. Biol. Chem. 264, 11754–11761.CrossRefGoogle Scholar
Fraser, M. J. (1992). The baculovirus-infected insect cell as a eukaryotic gene expression system. Curr. Topics Microbiol. Immunol. 158, 131–172.Google ScholarPubMed
Frommer, W. B., Hummel, S. & Riesmeier, J. W. (1993). Expression cloning in yeast of a cDNA encoding a broad specificity amino acid permease from Arabidopsis thaliana. Proc. Natl. Acad. Sci. 90, 5944–5948.CrossRefGoogle ScholarPubMed
Fuerst, T. R., Niles, E. G., Studier, F. W. & Moss, B. (1986). Eukaryotic transientexpression system based on recombinant Vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA 83, 8122–8126.CrossRefGoogle ScholarPubMed
Furth, P. A., Onge, L. S., Böger, H., Gruss, P., Gossen, M., Kistner, A., Bujard, H. & Hennighausen, L. (1994). Temporal control of gene expression in transgenic mice by a tetracycline-responsive promoter. Proc. Natl. Acad. Sci. USA 91, 9302–9306.CrossRefGoogle ScholarPubMed
George, S. T., Arbabian, M. A., Ruoho, A. E., Kiely, J. & Malbon, C. C. (1989). High-efficiency expression of mammalian β-adrenergic receptors in baculovirusinfected insect cells. Biochem. Biophys. Res. Commun. 163, 1265–1269.CrossRefGoogle ScholarPubMed
Germann, U. A., Willingham, M. C., Pastan, I. & Gottesman, M. M. (1990). Expression of the human multidrug transporter in insect cells by a recombinant baculovirus. Biochemistry 29, 2295–2303.CrossRefGoogle ScholarPubMed
Gether, U., Marray, T., Schwartz, T. W. & Johansen, T. E. (1992). Stable expression of high affinity NK1 (substance P) and NK2 (neurokinin A) receptors but low affinity NK3 (neurokinin B) receptors in transfected CHO cells. FEBS Lett. 296, 241–244.CrossRefGoogle ScholarPubMed
Goosen, M. F. A., Dauglis, A. J. & Faulkner, P. (1993). Insect cell culture engineerin. New York: Marcel Dekker.Google Scholar
Gossen, M., Bonin, A. L. & Bujard, H. (1994). Control of gene activity in higher eukaryotic cells by prokaryotic regulatory elements. TIBTECH 12, 58–62.CrossRefGoogle Scholar
Gould, G. W. (ED.) (1994). Membrane protein expression systems - A user's guide. London: Portland Press.Google Scholar
Greaves, D. R., Wilson, F. D., Lang, G. & Kioussis, D. (1989). Human CD2 3′-flanking sequences confer high-level, T cell-specific, position-independent gene expression in transgenic mice. Cell 56, 979–986.CrossRefGoogle ScholarPubMed
Green, T., Stauffer, K. A. & Lummis, S. C. R. (1995). Expression of recombinant homo-oligomeric 5-HT3 receptors provides new insights into their maturation and structure. J. Biol. Chem. 270, 6056–6061.CrossRefGoogle Scholar
Greenfield, C., Patel, G., Clark, S., Jones, N. & Waterfield, M. D. (1988). Expression of the human EGF receptor with ligand-stimulatable kinase activity in insect cells using a baculovirus vector. EMBO J. 7, 139–146.CrossRefGoogle ScholarPubMed
Grisshammer, R., Duckworth, R. & Henderson, R. (1993). Expression of a rat neurotensin receptor in Escherichia coli. Biochem. J. 295, 571–576.CrossRefGoogle ScholarPubMed
Grisshammer, R., Little, J. & Aharony, D. (1994). Expression of rat NK-2 (neurokinin A) receptor in E. coli. Receptors and Channels 2, 295–302.Google ScholarPubMed
Gropp, F. & Betlach, M. C. (1994). The bat gene of Halobacterium halobium encodes a trans-acting oxygen inducibility factor. Proc. Natl. Acad. Sci. USA 91, 5475–5479.CrossRefGoogle ScholarPubMed
Gropp, R., Gropp, F. & Betlach, M. C. (1992). Association of the halobacterial 7S RNA to the polysome correlates with the expression of the membrane protein bacterioopsin. Proc. Natl. Acad. Sci. USA 89, 1204–1208.CrossRefGoogle Scholar
Groves, J. D. & Tanner, M. J. A. (1992). Glycophorin A facilitates the expression of human band 3-mediated anion transport in Xenopus oocytes. J. Biol. Chem. 267, 22163–22170.CrossRefGoogle ScholarPubMed
Groves, J. D. & Tanner, M. J. A. (1994). The effects of glycophorin A on the expression of the human red cell anion transporter (Band 3) in Xenopus oocytes. J. Membrane Biol. 140, 81–88.CrossRefGoogle ScholarPubMed
Gu, H., Wall, S. C. & Rudnick, G. (1994). Stable expression of biogenic amine transporters reveals differences in inhibitor sensitivity, kinetics, and ion dependence. J. Biol. Chem. 269, 7124–7130.CrossRefGoogle ScholarPubMed
Gu, Y., Franco, A. Jr., Gardner, P. D., Lansman, J. B., Forsayeth, J. R. & Hall, Z. W. (1990). Properties of embryonic and adult muscle acetylcholine receptors transiently expressed in COS cells. Neuron 5, 147–157.CrossRefGoogle ScholarPubMed
Guengerich, F. P., Brian, W. R., Sari, M.-A. & Ross, J. T. (1991). Expression of mammalian cytochrome P450 enzymes using yeast-based vectors. Methods Enzymol. 206, 130–145.CrossRefGoogle ScholarPubMed
Gunn, F. J., Tate, C. G. & Henderson, P. J. F. (1994). Identification of a novel sugar- H+ symport protein, FucP, for transport of L-fucose into Escherichia coli. Molec. Microbiol. 12, 799–809.CrossRefGoogle Scholar
Hackett, N. R., Krebs, M. P., Dassarma, S., Goebel, W., Rajbhandary, U. L. & Khorana, H. G. (1990). Nucleotide sequence of a high copy number plasmid from Halobacterium strain GRB. Nucleic Acids Res. 18, 3408.CrossRefGoogle ScholarPubMed
Hadfield, C., Raina, K. K., Shashi-Menon, K. & Mount, R. C. (1993). The expression and performance of cloned genes in yeasts. Mycol. Res. 97, 897–944.CrossRefGoogle Scholar
Haendler, B., Hechler, U., Becker, A. & Schleuning, W.-D. (1993). Expression of human endothelin receptor ETB by Escherichia coli transformants. Biochem. Biophys. Res. Comm. 191, 633–638.CrossRefGoogle ScholarPubMed
Hallenberger, S., Bosch, V., Angliker, H., Shaw, E., Klenk, H.-D. & Garten, W. (1992). Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature 360, 358–361.CrossRefGoogle ScholarPubMed
Hammond, C., Braakman, I. & Helenius, A. (1994). Role of N-linked oligosaccharide recognition, glucose trimming and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA 91, 913–917.CrossRefGoogle ScholarPubMed
Hammond, C. & Helenius, A. (1994). Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 266, 456–458.CrossRefGoogle ScholarPubMed
Hanada, K., Yamato, I. & Anraku, Y. (1987). Construction and properties of bifunctionally active membrane-bound fusion proteins. J. Biol. Chem. 262, 14100–14104.CrossRefGoogle ScholarPubMed
Hanada, K., Yamato, I. & Anraku, Y. (1988). Purification and reconstitution of Escherichia coli proline carrier using a site specifically cleavable fusion protein. J. Biol. Chem. 263, 7181–7185.CrossRefGoogle ScholarPubMed
Harada, Y., Senda, T., Sakamoto, T., Takamoto, K. & Ishibashi, T. (1994).Expression of octopus rhodopsin in Escherichia colt. J. Biochem. 115, 66–75.CrossRefGoogle Scholar
Harfst, E., Johnstone, A. P., Gout, I., Taylor, A. H., Waterfield, M. D. & Nussey, S. S. (1992). The use of the amplifiable high-expression vector PEE14 to study the interactions of autoantibodies with recombinant human thyrotropin receptor. Mol. Cell. Endocrinology 83, 117–123.CrossRefGoogle Scholar
Hartl, F.-U., Hlodan, R. & Langer, T. (1994). Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem. Sci. 19, 20–25.CrossRefGoogle ScholarPubMed
Hartl, F.-U. & Neupert, W. (1990). Protein sorting to mitochondria: Evolutionary conservations of folding and assembly. Science 247, 930–938.CrossRefGoogle ScholarPubMed
Havelka, W. A., Henderson, R., Heymann, J. A. W. & Oesterhelt, D. (1993). Projection structure of halorhodopsin from Halobacterium halobium at 6 Å resolution obtained by electron cryo-microscopy. J. Mol. Biol. 234, 837–846.CrossRefGoogle ScholarPubMed
Havelka, W. A., Henderson, R. & Oesterhelt, D. (1995). Three-dimensional structure of halorhodopsin at 7 Å resolution. J. Mol. Biol. 247, 726–738.CrossRefGoogle ScholarPubMed
He, X., Wu, X., Knauf, P. A., Tabak, L. A. & Melvin, J. E. (1993). Functional expression of the rat anion exchanger AE2 in insect cells by a recombinant baculovirus. Am. J. Physiol. 264, C1075–C1079.CrossRefGoogle ScholarPubMed
Heim, R., Iwata, T., Zvaritch, E., Adamo, H. P., Rutishauser, B., Strehler, E. E., Guerini, D. & Carafoli, E. (1992). Expression, purification and properties of the plasma membrane Ca2+ pump and its N-terminally trauncated 105-kDa fragment. J. Biol. Chem. 267, 24476–24484.CrossRefGoogle ScholarPubMed
Helenius, A. (1994). How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 5, 253–265.CrossRefGoogle ScholarPubMed
Henderson, P. J. F. & Macpherson, J. S. (1986). Assay, genetics, proteins, and reconstitution of proton-linked galactose, arabinose, and xylose transport systems of Escherichia coli. Methods Enzymol. 125, 387–429.CrossRefGoogle ScholarPubMed
Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E. & Downing, K. H. (1990). Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213, 899–929.CrossRefGoogle ScholarPubMed
Hennessey, E. S., Hashemzadeh-Bonehi, L., Hunt, L. A. & Broome-Smith, J. K. (1993). Assembly of eukaryotic class III (N-out, C-in) membrane proteins into the Escherichia coli cytoplasmic membrane. FEBS Lett. 331, 159–161.CrossRefGoogle ScholarPubMed
Heymann, J. A. W., Havelka, W. A. & Oesterhelt, D. (1993). Homologous overexpression of a light-driven anion pump in an archaebacterium. Molec. Microbiol. 7, 623–630.CrossRefGoogle Scholar
Hildebrandt, V., Fendler, K., Heberle, J., Hoffmann, A., Bamberg, E. & Büldt, G. (1993)– Bacteriorhodopsin expressed in Schizosaccharomyces pombe pumps protons through the plasma membrane. Proc. Natl. Acad. Sci. USA 90, 3578–3582.CrossRefGoogle ScholarPubMed
Hildebrandt, V., Polakowski, F. & Büldt, G. (1991). Purple fission yeast: Overexpression and processing of the pigment bacteriorhodopsin. Photochem. Photobiol. 54, 1009–1016.CrossRefGoogle Scholar
Hildebrandt, V., Ramezani-Rad, M., Swida, U., Wrede, P., Grzesiek, S., Primke, M. & Büldt, G. (1989). Genetic transfer of the pigment bacteriorhodopsin into the eukaryote Schizosaccharomyces pombe. FEBS Lett. 243, 137–140.CrossRefGoogle ScholarPubMed
Hill-Perkins, M. S. & Possee, R. D. (1990). A baculovirus expression vector derived from the basic protein promoter of Autographa californica nuclear polyhedrosis virus. J. Gen. Virol. 71, 971–976.CrossRefGoogle ScholarPubMed
Hink, W. F., Thomsen, D. R., Davidson, D. J., Meyer, A. L. & Castellino, F. J. (1991). Expression of three recombinant proteins using baculovirus vectors in 23 insect cell lines. Biotechnol. Prog. 7, 9–14.CrossRefGoogle ScholarPubMed
Hjelmeland, L. M. (1990). Solubilization of native membrane proteins. Methods Enzymol. 182, 253–264.CrossRefGoogle ScholarPubMed
Ho, B. Y., Karschin, A., Raymond, J. R., Branchek, T., Lester, H. A. & Davidson, N. (1992). Expression in animal cells of the 5-HT1A receptor by a vaccinia virus vector system. FEBS Lett. 301, 303–306.CrossRefGoogle ScholarPubMed
Hobe, S., Prytulla, S., Kühlbrandt, W. & Paulsen, H. (1994). Trimerization and crystallization of reconstituted light-harvesting chlorophyll a/b complex. EMBO J. 13, 3423–3429.CrossRefGoogle ScholarPubMed
Holmans, P. L., Shet, M. S., Martin-Wixtrom, C. A., Fisher, C. W. & Estabrook, R. W. (1994). The high-level expression in Escherichia coli of the membrane-bound form of human and rat cytochrome b5 and studies on their mechanism of function. Arch. Biochem. Biophys. 312, 554–565.CrossRefGoogle ScholarPubMed
Holmes, M., Pfeifer, F. & Dyall-Smith, M. (1994). Improved shuttle vectors for Haloferax volcanii including a dual-resistance plasmid. Gene 146, 117–121.CrossRefGoogle ScholarPubMed
Honda, Z.-I., Nakamura, M., Miki, I., Minami, M., Watanabe, T., Seyama, Y., Okado, H., Toh, H., Ito, K., Miyamoto, T. & Shimizu, T. (1991). Cloning by functional expression of platelet-activating factor receptor from guinea-pig lung. Nature 349, 342–346.CrossRefGoogle ScholarPubMed
Horowitz, B., Eakle, K. A., Scheiner-Bobis, G., Randolph, G. R., Chen, C. Y., Hitzeman, R. A. & Farley, R. A. (1990). Synthesis and assembly of functional mammalian Na, K-ATPase in yeast. J. Biol. Chem. 265, 4189–4192.CrossRefGoogle ScholarPubMed
Hsu, T.-A., Eiden, J. J. & Betenbaugh, M. J. (1992). Engineering the assembly pathway of the baculovirus-insect cell expression system. Ann. NY Acad. Sci. 208–217.Google Scholar
Hsu, T.-A., Eiden, J. J., Bourgarel, P., Meo, T. & Betenbaugh, M. J. (1994). Effects of co-expressing chaperone BiP on functional antibody production in the baculovirus system. Protein Express. Purif. 5, 595–603.CrossRefGoogle ScholarPubMed
Hu, Y., Rajan, L. & Schilling, W. P. (1994). Ca2+ signalling in Sf9 insect cells and the functional expression of a rat brain M5 muscarinic receptor. Am. J. Physiol. 266, C1736–C1743.CrossRefGoogle ScholarPubMed
Huang, H.-J., Liao, C.-F., Yang, B.-C. & Kuo, T.-T. (1992). Functional expression of rat M5 muscarinic acetylcholine receptor in yeast. Biochem. Biophys. Res. Commun. 182, 1180–1186.CrossRefGoogle ScholarPubMed
Huang, K.-S., Bayley, H., Liao, M.-J., London, E. & Khorana, H. G. (1981). Refolding of an integral membrane protein. J. Biol. Chem. 256, 3802–3809.CrossRefGoogle ScholarPubMed
Hurtley, S. M., Bole, D. G., Hoover-Litty, H., Helenius, A. & Copeland, C. S. (1989). Interactions of misfolded influenza virus haemagglutinin with binding protein (BiP). J. Cell Biol. 108, 2117–2126.CrossRefGoogle ScholarPubMed
Iizuka, M. & Fukuda, K. (1993). Purification of the bovine nicotinic acetylcholine receptor α-subunit expresssed in baculovirus infected cells. J. Biochem. 114, 140–147.CrossRefGoogle Scholar
Imamura, T., Araki, M., Miyanhara, A., Nakao, J., Yonemura, H., Ohtomo, N. & Matsubara, K. (1987). Expression of hepatitis B virus middle and large surface antigen genes in Saccharomyces cerevisiae. J. Virol. 61, 3543–3549.CrossRefGoogle ScholarPubMed
Itoh, Y., Hayakawa, T. & Fujisawa, Y. (1986). Expression of hepatitis virus surface antigen P31 gene in yeast. Biochem. Biophys. Res. Commun. 138, 268–274.CrossRefGoogle ScholarPubMed
Jabbar, M. A. & Nayak, D. P. (1987). Signal processing, glycosylation, and secretion of mutant hemagglutinins of a human influenza virus by Saccharomyces cerevisiae. Mol. Cell. Biol. 7, 1476–1485.Google ScholarPubMed
Jabbar, M. A., Sivasubramanian, N. & Nayak, D. P. (1985). Influenza viral (A/WSN/33) hemagglutinin is expressed and glycosylated in the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 82, 2019–2023.CrossRefGoogle ScholarPubMed
Jackson, M. R., Cohen-Doyle, M. F., Peterson, P. A. & Williams, D. B. (1994). Regulation of MHC class 1 transport by the molecular chaperone, calnexin (p88, IP90). Science 263, 384–387.CrossRefGoogle Scholar
Jansen, J. J. M., Mulder, W. R., De Caluwe, G. L. J., Vlak, J. M. & De Grip, W. J. (1991). In vitro expression of bovine opsin using recombinant baculovirus: the role of glutamic acid (134) in opsin biosynthesis and glycosylation. Biochim. Biophys. Acta 1089, 68–76.CrossRefGoogle ScholarPubMed
Jansen, K. U., Conroy, W. G., Claudio, T., Fox, T. D., Fujita, N., Hamill, O., Lindstrom, J. M., Luther, M., Nelson, N., Ryan, K. A., Sweet, M. T. & Hess, G. P. (1989). Expression of the four subunits of the Torpedo californica nicotinic acetylcholine receptor in Saccharomyces cerevisiae. J. Biol. Chem. 264, 15022–15027.CrossRefGoogle ScholarPubMed
Janssen, J. J. M., Van De Ven, W. J. M.Van Groningen-Luyben, W. A. H. M., Roosien, J., Vlak, J. M. & De Grip, W. J. (1988). Synthesis of functional bovine opsin in insect cells under the control of the baculovirus polyhedrin promoter. Mol. Biol. Rep. 13, 65–71.CrossRefGoogle ScholarPubMed
Jap, B. K., Zulauf, M., Scheybani, T., Hefti, A., Baumeister, W., Aebi, U. & Engel, A. (1992). 2D crystallization: from art to science. Ultramicroscopy 46, 45–84.CrossRefGoogle ScholarPubMed
Jarvie, K. R., Tiberi, M., Silvia, C., Gingrich, J. A. & Caron, M. G. (1993). Molecular cloning, stable expression and desensitization of the human dopamine D1B/D5 receptor. J. Receptor Research 13, 573–590.CrossRefGoogle Scholar
Jarvis, D. L. (1992). Baculovirus expression vectors. A review and update. Ann. Ny Acad. Sci. 240–247.Google Scholar
Jarvis, D. L., Fleming, J.-A. G. W., Kovacs, G. R., Summers, M. D. & Guarino, L. A. (1990). Use of early baculovirus promoters for continuous expression and efficient processing of foreign gene products in stably transformed lepidopteran cells. Bio/Technology 8, 950–955.Google ScholarPubMed
Jarvis, D. L. & Summers, M. D. (1989). Glycosylation and secretion of human tissue plasminogen activator in recombinant baculovirus-infected insect cells. Mol. Cell. Biol. 9, 214–223.Google ScholarPubMed
Javitch, J. A., Kaback, J., LI, X. & Karlin, A. (1994). Expression and characterisation of human dopamine D2 receptor in baculovirus-infected insect cells. J. Receptor Res. 14, 99–117.CrossRefGoogle ScholarPubMed
Jelinek, L. J., Lok, S., Rosenberg, G. B., Smith, R. A., Grant, F. J., Biggs, S., Bensch, P. A., Kuijper, J. L., Sheppard, P. O., Sprecher, C. A., O'Hara, P. J., Foster, D., Walker, K. M., Chen, L. H. J., McKernan, P. A. & Kindsvogel, W. (1993). Expression cloning and signaling properties of the rat glucagon receptor. Science 259, 1614–1616.CrossRefGoogle ScholarPubMed
Jensen, R. A., Beeler, J. F., Heidaran, M. A. & Larochelle, W. J. (1992). Characterisation of baculovirus-expressed human α anβ platelet-derived growth factor receptors. Biochemistry 31, 10887–10892.CrossRefGoogle Scholar
Jin, H., Oksenberg, D., Ashkenazi, A., Peroutka, S. J., Duncan, A. M. V., Rozmahel, R., Yang, Y., Mengod, G., Palacios, J. M. & O'Dowd, B. F. (1992). Characterization of the human 5-hydroxytryptamineiB receptor. J. Biol. Chem. 267, 5735–5738.CrossRefGoogle ScholarPubMed
Johnson, E. F., Walker, D. L., Griffin, K. J., Clark, J. E., Okita, R. T., Muerhoff, A. S. & Masters, B. S. (1990). Cloning and expression of three rabbit kidney cDNAs encoding lauric acid ω-hydroxylases. Biochemistry 29, 873–879.CrossRefGoogle ScholarPubMed
Johnson, R. L., Vaughan, R. A., Caterina, M. J., van Haastert, P. J. M. & Devreotes, P. N. (1991). Overexpression of the cAMP receptor 1 in growing Dictyostelium cells. Biochemistry 30, 6982–6986.CrossRefGoogle ScholarPubMed
Joyce, K. A., Atkinson, A. E., Bermudez, I., Beadle, D. J. & King, L. A. (1993). Synthesis of GABA-A receptors in stable insect cell lines. FEBS Lett. 335, 61–64.CrossRefGoogle Scholar
Karrasch, S., Bullough, P. A. & Ghosh, R. (1995). The 85 Å projection map of the light-harvesting complex I from Rhodospirillum rubrum reveals a ring composed of 16 subunits. EMBO J. 14, 631–638.CrossRefGoogle ScholarPubMed
Karnik, S. S., Nassal, M., Doi, T., Jay, E., Sgaramella, V. & Khorana, H. G. (1987). Structure-function studies on bacteriorhodopsin-II. Improved expression of the bacterio-opsin gene in Escherichia coli. J. Biol. Chem. 262, 9255–9263.CrossRefGoogle ScholarPubMed
Karnik, S. S., Ridge, K. D., Bhattacharya, S. & Khorana, H. G. (1993). Palmitoylation of bovine opsin and its cysteine mutants in COS cells. Proc. Nad. Acad. Sci. USA 90, 40–44.CrossRefGoogle ScholarPubMed
Kartner, N., Hanrahan, J. W., Jensen, T. J., Naismith, A. L., Sun, S., Ackerley, C. A., Reyes, E. F., Tsui, L.-C., Rommens, J. M., Bear, C. & Riordan, J. R. (1991). Expression of the cystic fibrosis gene in non-epithelial invertebrate cells produces a regulated anion conductance. Cell 64, 681–691.CrossRefGoogle ScholarPubMed
Kaushal, S., Ridge, K. D. & Khorana, H. G. (1994). Structure and function in rhodopsin: the role of asparagine-linked glycosylation. Proc. Natl. Acad. Sci. USA 91, 4024–4028.CrossRefGoogle ScholarPubMed
Kawamoto, S., Hattori, S., Oiji, I., Hamajima, K., Mishina, M. & Okuda, K. (1994). Ligand binding properties and N-glycosylation of α1 subunit of the AMPA-selective glutamate receptor channel expressed in baculovirus system. Eur. J. Biochem. 223, 665–673.CrossRefGoogle Scholar
Kawamoto, S., Hattori, S., Oiji, I., Ueda, A., Fukushima, J., Sakimura, K., Mishina, M. & Okuda, K. (1993). Expression of the α2 and α2 subunits of the AMPA-selective glutamate receptor channel in insect cells using a baculovirus vector. Ann. N. Y. Acad. Sci. 707, 460–462.CrossRefGoogle Scholar
Kawamoto, S., Onishi, H., Hattori, S., Miyagi, Y., Amaya, Y., Mishina, M. & Okuda, K. (1991). Functional expression of the α1 subunit of the AMPA-selective glutamate receptor channel using a baculovirus system. Biochem. Biophys. Res. Commun. 181, 756–763.CrossRefGoogle Scholar
Keinanen, K., Kohr, G., Seeburg, P. H., Laukkanen, M.-L. & Oker-Blom, C. (1994). High-level expression of functional glutamate receptor channels in insect cells. Bio/Technology 12, 802–806.Google ScholarPubMed
Kellerman, O. K. & Ferenci, T. (1982). Maltose-binding protein from Escherichia coli. Methods Enzymol. 90, 459–463.CrossRefGoogle Scholar
Khorana, H. G. (1988). Bacteriorhodopsin, a membrane protein that uses light to translocate protons. J. Biol. Chem. 263, 7439–7442.CrossRefGoogle ScholarPubMed
King, K., Dohlman, H. G., Thorner, J., Caron, M. G. & Lefkowitz, R. J. (1990). Control of yeast mating signal transduction by a mammalian β2-adrenergic receptor and Gs α subunit. Science 250, 121–123.CrossRefGoogle Scholar
King, L. A. & Possee, R. D. (1992). The Baculovirus Expression System: A Laboratory Guide. London: Chapman & Hall.CrossRefGoogle Scholar
Kitts, P. A. & Possee, R. D. (1993). A method for producing recombinant baculovirus expression vectors at high frequency. Biotechniques 14, 810–817.Google ScholarPubMed
Klaasen, C. H. W., van Uem, T. J. F., De Moel, M. P., De Caluwe, G. L. J., Swarts, H. G. P. & De Pont, J. J. H. H. M. (1993). Functional expression of gastric H, K-ATPase using the baculovirus expression system. FEBS Lett. 329, 277–282.CrossRefGoogle Scholar
Klaiber, K., Williams, N., Roberts, T. M., Papazian, D. M., Jan, L. Y. & Miller, C. (1990). Functional expression of Shaker K+ channels in a baculovirus-infected insect cell line. Neuron 5, 221–226.CrossRefGoogle Scholar
Kleymann, G., Boege, F., Hahn, M., Hampe, W., Vasudevan, S. & Reiländer, H. (1993). Human β2-adrenergic receptor produced in stably transformed insect cells is functionally coupled via endogenous GTP-binding protein to adenylyl cyclase. Eur. J. Biochem. 213, 797–804.CrossRefGoogle Scholar
Kleymann, G., Ostermeier, C., Ludwig, B., Skerra, A. & Michel, H. (1995). Engineered Fv fragments as a tool for the one-step purification of integral multisubunit membrane protein complexes. Bio/Technology 13, 155–160.Google ScholarPubMed
Koehler, J. E., Birkelund, S. & Stephens, R. S. (1992). Overexpression and surface localization of the Chlamydia trachomatis major outer membrane protein in Escherichia coli. Molec. Microbiol. 6, 1087–1094.Google Scholar
Kolansky, D. M., Brines, M. L., Gilmore-Hebert, M. & Benz, E. J. Jr. (1992). The A2 isoform of rat Na+, K++-adenosine triphosphatase is active and exhibits high ouabain affinity when expressed in transfected fibroblasts. FEBS Lett. 303, 147–153.Google ScholarPubMed
Kozak, M. (1991). Structural features in eukaryotic mRNAs that modulate the initiation of translation. J. Biol. Chem. 266, 19867–19870.CrossRefGoogle ScholarPubMed
Kozak, M. (1992). Regulation of translation in eukaryotic systems. Annu. Rev. Cell Biol. 8, 197–225.CrossRefGoogle ScholarPubMed
Krebs, M. P., Hauss, T., Heyn, M. P., Rajbhandary, U. L. & Khorana, H. G. (1991). Expression of the bacterioopsin gene in Halobacterium halobium using a multicopy plasmid. Proc. Natl. Acad. Sci. USA 88, 859–863.CrossRefGoogle ScholarPubMed
Krebs, M. P., Mollaaghababa, R. & Khorana, H. G. (1993 a). Gene replacement in Halobacterium halobium and expression of bacteriorhodopsin mutants. Proc. Natl. Acad. Sci. USA 90, 1987–1991.CrossRefGoogle ScholarPubMed
Krebs, M. P., Spudich, E. N., Khorana, H. G. & Spudich, J. L. (1993 b). Synthesis of a gene for sensory rhodopsin I and its functional expression in Halobacterium halobium. Proc. Natl. Acad. Sci. USA 90, 3486–3490.CrossRefGoogle ScholarPubMed
Kretzschmar, E., Geyer, R. & Klenk, H.-D. (1994). Baculovirus infection does not alter N-glycosylation in Spodoptera frugiperda cells. Biol. Chem. Hoppe-Seyler 375, 323–327.CrossRefGoogle Scholar
Kriegler, M. (1990). Gene transfer and expression- A laboratory manual. New York: Stockton Press.CrossRefGoogle Scholar
Kubelka, V., Altmann, F., Kornfeld, G. & Marz, L. (1994). Structures of the Nlinked oligosaccharides of the membrane glycoproteins from three lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N). Arch. Biochem. Biophys. 308, 148–157.CrossRefGoogle ScholarPubMed
Kuchler, K. & Thorner, J. (1992). Functional expression of human i in the yeast Saccharomyces cerevisiae. Proc. Natl. Acad Sci. USA 89, 2302–2306.CrossRefGoogle Scholar
Kühlbrandt, W. (1988). Three-dimensional crystallization of membrane proteins. Q. Rev. Biophys. 21, 429–477.CrossRefGoogle ScholarPubMed
Kühlbrandt, W. (1992). Two-dimensional crystallization of membrane proteins. Q. Rev. Biophys. 25, 1–49.CrossRefGoogle ScholarPubMed
Kühlbrandt, W., WANG, D. N. & Fujiyoshi, Y. (1994). Atomic model of plant lightharvesting complex by electron crystallography. Nature 367, 614–621.CrossRefGoogle ScholarPubMed
Kukuruzinska, M. A., Bergh, M. L. E. & Jackson, B. L. (1987). Protein glycosylation in yeast. Ann. Rev. Biochem. 56, 915–944.CrossRefGoogle ScholarPubMed
Kuroda, K., Geyer, H., Geyer, R., Doerfler, W. & Klenk, H.-D. (1990). The oligosaccharides of influenza virus hemagglutinin expressed in insect cells by a baculovirus vector. Virology 174, 418–429.CrossRefGoogle ScholarPubMed
Kuroda, K., Hauser, C., Rott, R., Klenk, H.-D. & Doerfler, W. (1986). Expression of the influenza virus haemagglutinin in insect cells by a baculovirus vector. EMBO J. 5. 1359–1365.CrossRefGoogle ScholarPubMed
Kutay, U., Ahnert-Hilger, G., Hartmann, E., Wiedenmann, B. & Rapoport, T. A. (1995). Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum. EMBO J. 14, 217–223.CrossRefGoogle Scholar
Kuwano, M., Seguchi, T. & Ono, M. (1991). Glycosylation mutations of serine/threonine-linked oligosaccharides in low density lipoprotein receptor: indispensable roles of O-glycosylation. J. Cell Sci. 98, 131–134.CrossRefGoogle ScholarPubMed
Kwatra, M. M., Schwinn, D. A., Schreurs, J., Blank, J. L., Kim, C. M., Benovic, J. L., Krause, J. E., Caron, M. G. & Lefkowitz, R. J. (1993). The substance Preceptor, which couples to Gq11, is a substrate of βadrenergic receptor kinase 1 and 2. J. Biol. Chem. 268, 9161–9164.CrossRefGoogle Scholar
Lam, W. L. & Doolittle, W. F. (1989). Shuttle vectors for the archaebacterium Halobacterium volcanii. Proc. Natl. Acad. Sci. USA 86, 5478–5482.CrossRefGoogle ScholarPubMed
Langley, K. E., Egan, K. M., Barendt, J. M., Parker, C. G. & Bitter, G. A. (1988). Characterization of purified hepatitis B surface antigen containing pre-S(2) epitopes expressed in Saccharomyces cerevisiae. Gene 67, 229–245.CrossRefGoogle ScholarPubMed
Lanyi, J. K. (1992). Proton transfer and energy coupling in the bacteriorhodopsin photocycle. J. Bioenergetics Biomembranes 24, 169–179.CrossRefGoogle ScholarPubMed
Larson, J. R., Coon, M. J. & Porter, T. D. (1991). Alcohol-inducible cytochrome P-450IIE1 lacking the hydrophobic NH2-terminal segment retains catalytic activity and is membrane-bound when expressed in Escherichia coli. J. Biol. Chem. 266, 7321–7324.CrossRefGoogle ScholarPubMed
Laussermair, E. & Oesterhelt, D. (1992). A system for site-specific mutagenesis of the photosynthetic reaction center in Rhodopseudomonas viridis. EMBO J. 11, 777–783.CrossRefGoogle ScholarPubMed
Lazdunski, A. M. (1989). Peptidases and proteases of Escherichia coli and Salmonella typhimurium. FEMS Microbiol. Reviews 63, 265–276.Google Scholar
Le Maire, M., Deschamps, S., Moller, J. V., Le Caer, J. P. & Rossier, J. (1993). Electrospray ionization mass spectrometry on hydrophobic peptides electroeluted from sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Application to the topology of the sarcoplasmic reticulum Ca2+-ATPase. Anal. Biochem. 214, 50–57.CrossRefGoogle Scholar
Lee, H.-J., Rocheleau, T., Zhang, H.-G., Jackson, M. B. & Ffrench-Constant, R. H. (1993). Expression of a Drosophila GABA receptor in a baculovirus insect cell system. FEBS Lett. 335, 315–318.CrossRefGoogle Scholar
Lee, J.-I., Kuhn, A. & Dalbey, R. E. (1992). Distinct domains of an oligotopic membrane protein are sec-dependent and sec-independent for membrane insertion. J. Biol. Chem. 267, 938.Google ScholarPubMed
Lesage, F., Attali, B., Lakey, J., Honore, E., Romey, G., Faurobert, E., Lazdunski, M. & Barhanin, J. (1993). Are Xenopus oocytes unique in displaying functional IsK channel heterologous expression? Receptors Channels 1, 143–152.Google ScholarPubMed
Li, S.-L., YAN, P.-F., Paz, I. B. & Fujita-Yamaguchi, Y. (1992 a). Human insulin receptor β subunit transmembrane/cytoplasmic domain expressed in a baculovirus expression system: purification, characterisation and polylysine effects on the protein tyrosine kinase activity. Biochemistry 31, 12455–12462.CrossRefGoogle Scholar
Li, Z., Smith, C. D., Smolley, J. R., Bridge, J. H. B., Frank, J. S. & Philipson, K. D. (1992 b). Expression of the cardiac Na+Ca2+ exchanger in insect cells using a baculovirus vector. J. Biol. Chem. 267, 7828–7833.CrossRefGoogle ScholarPubMed
Liljeström, P. & Garoff, H. (1991). A new generation of animal cell expression vectors based on the Semliki Forest virus replicon. Bio/Technology 9, 1356–1361.CrossRefGoogle ScholarPubMed
Lis, H. & Sharon, N. (1993). Protein glycosylation. Structural and functional aspects. Eur. J. Biochem. 218, 1–27.CrossRefGoogle ScholarPubMed
Liscum, L., Finer-Moore, J., Stroud, R. M., Luskey, K. L., Brown, M. S. & Goldstein, J. L. (1985). Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum. J. Biol. Chem. 260, 522–530.CrossRefGoogle Scholar
Ljungdahl, P. O., Gimeno, C. J., Styles, C. A. & Fink, G. R. (1992). SHR3: a novel component of the secretory pathway specifically required for localization of amino acid permeases in yeast. Cell 71, 463–478.CrossRefGoogle ScholarPubMed
Loddenkötter, B., Kammerer, B., Fischer, K. & Flugge, U. I. (1993). Expression of the functional mature chloroplast triose phosphate translocator in yeast internal membranes and purification of the histidine-tagged protein by a single metal-affinity chromatography step. Proc. Natl. Acad. Sci. USA 90, 2155–2159.CrossRefGoogle ScholarPubMed
Lohse, M. J. (1992). Stable overexpression of human β2-adrenergic receptors in mammalian cells. Naunyn-Schmiedeberg's Arch. Pharmacol. 345, 444–451.CrossRefGoogle Scholar
Loo, T. P. & Clarke, D. M. (1994 a). Functional expression of human renal Na+/Ca2+ exchanger in insect cells. Am. J. Physiol. 267, F70–F74.Google ScholarPubMed
Loo, T. W. & Clarke, D. M. (1994 b). Prolonged association of temperature-sensitive mutants of human P-glycoprotein with calnexin during biogenesis J. Biol. Chem. 269, 28683–28689.CrossRefGoogle Scholar
Lopez Garcia, M. P., Dansette, P. M., Valadon, P., Amar, C., Beaune, P. H., Guengerich, F. P. & Mansuy, D. (1993). Human-liver cytochromes P-450 expressed in yeast as tools for reactive-metabolite formation studies. Eur. J. Biochem. 213, 223–232.CrossRefGoogle ScholarPubMed
Luckow, V. A. (1994). Baculovirus systems for the expression of human gene products. Current Opinion Biotechnol. 4, 564–572.CrossRefGoogle Scholar
Lundström, K., Mills, A., Buell, G., Allet, E., Adami, N. & Liljeström, P. (1994). High-level expression of the human neurokinin-1 receptor in mammalian cell lines using the Semliki Forest virus expression system. Eur. J. Biochem. 224, 917–921.CrossRefGoogle ScholarPubMed
Ma, T., Frigeri, A., Tsai, S.-T., Verbavatz, J.-M. & Verkman, A. S. (1993). Localization and functional analysis of CHIP28k water channels in stably transfected Chinese Hamster Ovary cells, J. Biol. Chem. 268, 22756–22764.CrossRefGoogle ScholarPubMed
Mackett, M. (1994). Expression cf membrane proteins using vaccinia recombinants. In Membrane protein expression systems. A user's guide, (ed. Gould, G. W.), pp. 125–175. London: Portland Press.Google Scholar
Mahanty, S. K., Rao, U. S., Nicholas, R. A. & Scarborough, G. A. (1994). High yield expression of the Neurospora crassa plasma membrane H+-ATPase in Saccharomyces cerevisiae. J. Biol. Chem. 269, 17705–17712.CrossRefGoogle ScholarPubMed
Maiden, M. C. J., Jones-Mortimer, M. C. & Henderson, P. J. F. (1988). The cloning, DNA sequence, and overexpression of the gene araE coding for arabinose-proton symport in Escherichia coli K12. J. Biol. Chem. 263, 8003–8010.CrossRefGoogle ScholarPubMed
Manneberg, M., Friedlein, A., Kurth, H., Lahm, H.-W. & Fountoulakis, M. (1994). Structural analysis and localization of the carbohydrate moieties of a soluble human interferon receptor produced in baculovirus cells. Protein Sci. 3, 30–38.CrossRefGoogle ScholarPubMed
Maricq, A. V., Peterson, A. S., Brake, A. J., Myers, R. M. & Julius, D. (1991). Primary structure and functional expression of the 5HTM3 receptor, a serotonin-gated ion channel. Science 254, 432–437.CrossRefGoogle ScholarPubMed
Marullo, S., Delavier-Klutchko, C., Guillet, J.-G., Charbit, A., Strosberg, A. D. & Emorine, L. J. (1989). Expression of human β1 and β2 adrenergic receptors in E. coli as a new tool for ligand screening. Bio/Technology 7, 923–927.Google Scholar
Maruyama, K. & Maclennan, D. H. (1988). Mutation of aspartic acid-351, lysine-352, and lysine-515 alters the Ca2+ transport activity of the Ca2+-ATPase expressed in COS-1 cells. Proc. Natl. Acad. Sci. USA 85, 3314–3318.CrossRefGoogle ScholarPubMed
Matsudaira, P. (1987). Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035–10038.CrossRefGoogle ScholarPubMed
Matsuyama, S.-I., Akimaru, J. & Mizushima, S. (1990). SecE-dependent overproduction of SecY in Escherichia coli. FEBS Lett. 269, 96–100.CrossRefGoogle Scholar
Maurizi, M. R. (1992). Proteases and protein degradation in Escherichia coli. Experientia 48, 178–201.Google Scholar
Mazina, K. E., Strader, C. D. & Fong, T. M. (1994). Expression and solubilisation of a recombinant human neurokinin-1 receptor in insect cells. J. Receptor Res. 14, 63–73.CrossRefGoogle ScholarPubMed
McAllister, G., Charlesworth, A., Snodin, C., Beer, M. S., Noble, A. J., Middlemiss, D. N., Iversen, L. L. & Whiting, P. (1992). Molecular cloning of a serotonin receptor from human brain (5HT1E): A fifth 5HT1-like subtype. Proc. Natl. Acad. Sci. USA 89, 5517–5521.CrossRefGoogle ScholarPubMed
McDermott, G., Prince, S. M., Freer, A. A., Hawthornthwaite, A. M., Papiz, M. Z., Cogdell, R. J. & Isaacs, N. W. (1995). Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria. Nature 374, 517–521.CrossRefGoogle Scholar
Meerman, H. J. & Georgiou, G. (1994). Construction and characterization of a set of E. coli strains deficient in all known loci affecting the proteolytic stability of secreted recombinant proteins. Bio/Technology 12, 1107–1110.CrossRefGoogle ScholarPubMed
Melikian, H. E., McDonald, J. K., Gu, H., Rudnick, G., Moore, K. R. & Blakely, R. D. (1994). Human norepinephrine transporter. J. Biol. Chem. 269, 12290–12297.CrossRefGoogle ScholarPubMed
Meyer, T. H., Van Endert, P. M., Uebel, S., Ehring, B. & Tampe, R. (1994). Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells. FEBS Lett. 351, 443–447.CrossRefGoogle ScholarPubMed
Michel, H. (1990). Crystallizing membrane proteins: experiments on different systems. In Crystallization of Membrane Proteins, (ed. Michel, H.), pp. 73–78. Boca Raton, Florida: CRC Press.Google Scholar
Miercke, L. J. W., Betlach, M. C., Mitra, A. K., Shand, R. F., Fong, S. K. & Stroud, R. M. (1991). Wild-type and mutant bacteriorhodopsins D85N, D96N, and R82Q: Purification to homogeneity, pH dependence of pumping, and electron diffraction. Biochemistry 30, 3088–3098.CrossRefGoogle ScholarPubMed
Miller, C., Moczydlowski, E., Latorre, R. & Phillips, M. (1985). Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscle. Nature 313, 316–318.CrossRefGoogle ScholarPubMed
Miller, D. B., Munster, D., Wasvary, J. S., Simke, J. P., Peppard, J. V., Bowen, B. R. & Marshall, P. J. (1994). The heterologous expression and characterization of human prostaglandin G/H synthase-2 (COX-2). Biochem. Biophys. Res. Commun. 201, 356–362.CrossRefGoogle Scholar
Mills, A., Allet, B., Bernard, A., Chabert, C., Brandt, E., Cavegn, C., Chollet, A. & Kawashima, E. (1993). Expression and characterisation of human dopamine D4 receptors in baculovirus-infected insect cells. FEBS Lett. 320, 130–134.CrossRefGoogle ScholarPubMed
Mitra, A. K., Miercke, L. J. W., Turner, G. J., Shand, R. F., Betlach, M. C. & Stroud, R. M. (1993). Two-dimensional crystallization of Escherichia coli-expressed bacteriorhodopsin and its D96N variant: High resolution structural studies in projection. Biophys. J. 65, 1295–1306.CrossRefGoogle ScholarPubMed
Moir, D. T. & Davidow, L. S. (1991). Production of proteins by secretion from yeast. Methods Enzymol. 194, 491–507.CrossRefGoogle ScholarPubMed
Moller, J. V., Le Maire, M. & Anderson, J. P. (1986). Uses of non-ionic and bile salt detergents in the study of membrane proteins. In Progress in Protein-Lipid Interactions, Vol 2, (ed. Watts, & De Pont, ), pp. 147–196. Elsevier.Google Scholar
Moriyama, Y., Iwamoto, A., Hanada, H., Maeda, M. & Futai, M. (1991). One-step purification of Escherichia coli H+-ATPase (F0F1) and its reconstitution into liposomes with neurotransmitter transporters. j. Biol. Chem. 266, 22141–22146.CrossRefGoogle ScholarPubMed
Moss, B. (1991). Vaccinia virus: A tool for research and vaccine development. Science 252, 1662–1667.CrossRefGoogle ScholarPubMed
Mouillac, B., Caron, M., Bonin, H., Dennis, M. & Bouvier, M. (1992). Agonistmodulated palmitoylation of β2-adrenergic receptor in Sf9 cells. J. Biol. Chem. 267, 21733–21737.CrossRefGoogle Scholar
Mulheron, J. G., Casanas, S. J., Arthur, J. M., Garnovskaya, M. N., Gettys, T. W. & Raymond, J. R. (1994). Human 5-HT1A receptor expressed in insect cells activates endogenous G0-like G protein(s). J. Biol. Chem. 269, 12954–12962.CrossRefGoogle Scholar
Murakami, H., Blobel, G. & Pain, D. (1993). Signal sequence region of mitochondrial precursor proteins binds to mitochondrial import receptor. Proc. Natl. Acad. Sci. USA 90, 3358–3362.CrossRefGoogle ScholarPubMed
Murdza-Inglis, D. L., Patel, H. V., Freeman, K. B., Jezek, P., Orosz, D. E. & Garlid, K. D. (1991). Functional reconstitution of rat uncoupling protein following its high level expression in yeast. J. Biol. Chem. 260, 11871–11875.CrossRefGoogle Scholar
Murhammer, D. W. & Goochee, C. F. (1988). Scaleup of insect cell cultures: protective effects of pluronic F-68. Bio/Technology 6, 1411–1418.Google Scholar
Nakamoto, R. K., RAO, R. & Slayman, C. W. (1991). Expression of the yeast plasma membrane H+-ATPase in secretory vesicles. J. Biol. Chem. 266, 7940–7949.CrossRefGoogle ScholarPubMed
Namba, H., Yamashita, S., Usa, T., Kimura, H., Yokoyama, N., Izumi, M. & Nagataki, S. (1993). Overexpression of the intact thyrotropin receptor in a human thyroid carcinoma cell line. Endocrinology 132, 839–845.CrossRefGoogle Scholar
Nassal, M., Mogi, T., Karnik, S. S. & Khorana, H. G. (1987). Structure-function studies on bacteriorhodopsin - III. Total synthesis of a gene for bacterio-opsin and its expression in Escherichia coli. J. Biol. Chem. 262, 9264–9270.CrossRefGoogle Scholar
Ng, G. Y. K., George, S. R., Zastawny, R. L., Caron, M., Bouvier, M., Dennis, M. & O'Dowd, B. F. (1993). Human serotonin 1B receptor expression in Sf9 cells: phosphorylation, palmitoylation and adenyl cyclase inhibition. Biochemistry 32, 11727–11733.CrossRefGoogle Scholar
NG, G. Y. K., Mouillac, B., George, S. R., Caron, M., Dennis, M., Bouvier, M. & O'Dowd, B. F. (1994 a). Desensitization, phosphorylation, and palmitoylation of the human dopamine Di receptor. Eur. J. Pharmacol. 267, 7–19.CrossRefGoogle Scholar
Ng, G. Y. K., O'Dowd, B. F., Caron, M., Dennis, M., Brann, M. R. & George, S. R. (1994 b). Phosphorylation and palmitoylation of the human D2L dopamine receptor in Sf9 cells. J. Neurochem. 63, 1589–1595.CrossRefGoogle ScholarPubMed
Ni, B., Chang, M., Duschl, A., Lanyi, J. & Needleman, R. (1990). An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium. Gene 90, 169–172.Google Scholar
Nilsson, B., Forsberg, G., Moks, T., Hartmanis, M. & Uhlen, M. (1992). Fusion proteins in biotechnology and structural biology. Current Opinion Struct. Biol. 2, 569–575.CrossRefGoogle Scholar
Nishimoto, M., Clark, J. E. & Masters, B. S. S. (1993). Cytochrome P450 4A4: Expression in Escherichia coli, purification, and characterization of catalytic properties. Biochemistry 32, 8863–8870.CrossRefGoogle ScholarPubMed
Noiva, R. & Lennarz, W. J. (1992). Protein disulfide isomerase. J. Biol. Chem. 267, 3553–3556.CrossRefGoogle ScholarPubMed
O'Dowd, B., Hnatowich, M., Caron, M. G., Lefkowitz, R. J. & Bouvier, M. (1989). Palmitoylation of the human β2-adrenergic receptor. J. Biol. Chem. 264, 7564–7569.CrossRefGoogle Scholar
O'Neill, G. P., Mancini, J. A., Kargman, S., Yergey, J., Kwan, M. Y., Falgueyret, J.-P., Abramovitz, M., Kennedy, B. P., Ouellet, M., Cromlish, W., Culp, S., Evans, J. F., Ford-Hutchinson, A. W. & Vickers, P. J. (1994). Overexpression of human prostaglandin G/H synthase-1 and -2 by recombinant vaccinia virus: inhibition by nonsteroidal anti-inflammatory drugs and biosynthesis of 15-hydroxyeicosatetraenoic acid. Molec. Pharmacol. 45, 245–254.Google Scholar
O'Reilly, D. R., Miller, L. K. & Luckow, V. A. (1992). Baculovirus Expression Vectors: A Laboratory Manual. New York: W. H. Freeman & Co.Google Scholar
Ohta, D., Matsu-Ura, Y. & Sato, R. (1991). Expression and characterization of a rabbit liver cytochrome P450 belonging to P450IIB subfamily with the aid of the baculovirus expression vector system. Biochem. Biophys. Res. Commun. 175, 394–399.CrossRefGoogle ScholarPubMed
Okerblom, C., Jansson, C., Karp, M., Lindqvist, C., Savola, J. M., Vlak, J. & Akerman, K. (1993). Functional analysis of the human alpha-2c-c4 adrenergic receptor in insect cells expressed by a luciferase-based baculovirus vector. Biochim. Biophys. Acta 1176, 269–275.CrossRefGoogle ScholarPubMed
Oprian, D. D., Molday, R. S., Kaufman, R. J. & Khorana, H. G. (1987). Expression of a synthetic bovine rhodopsin gene in monkey kidney cells. Proc. Natl. Acad. Sci. USA 84, 8874–8878.CrossRefGoogle ScholarPubMed
Parker, E. M., Grisel, D. A., Iben, L. G., Nowak, H. P., Mahle, C. D., Yocca, F. D. & Gaughan, G. T. (1994). Characterization of human 5-HT1 receptors expressed in Sf9 insect cells. Eur. J. Pharmacol. 268, 43–53.CrossRefGoogle ScholarPubMed
Parker, E. M., Kameyama, K., Higashijima, T. & Ross, E. M. (1991). Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells. J. Biol. Chem. 266, 519–527.CrossRefGoogle ScholarPubMed
Parker, E. M. & Ross, E. M. (1991). Truncation of the extended carboxyl-terminal domain increases the expression and regulatory activity of the avian β-adrenergic receptor. J. Biol. Chem. 266, 9987–9996.CrossRefGoogle ScholarPubMed
Patterson, N. H. & Pauling, C. (1985). Evidence for two restriction-modification systems in Halobacterium cutirubrum. J. Bacteriol. 163, 783–784.CrossRefGoogle Scholar
Paul, J. I., Tavare, J., Denton, R. M. & Steiner, D. F. (1990). Baculovirus-directed expression of the human insulin receptor and insulin binding ectodomain. J. Biol. Chem. 265, 13074–13083.CrossRefGoogle ScholarPubMed
Paulsen, H., Rümler, U. & Rüdiger, W. (1990). Reconstitution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed in Escherichia coli. Planta 181, 204–211.Google Scholar
Paulson, J. C. (1989). Glycoproteins: what are the sugar chains for? Trends Biochem. Sci. 14, 272–276.CrossRefGoogle Scholar
Payette, P., Gossard, F., Whiteway, M. & Dennis, M. (1990). Expression and pharmacological characterisation of the human M1 muscarinic receptor in Saccharomyces cerevisiae. FEBS Lett. 266, 21–25.CrossRefGoogle Scholar
Peralta, E. G., Ashkenazi, A., Winslow, J. W., Ramachandran, J. & Capon, D. J. (1988). Differential regulation of PI hydrolysis and adenylyl cyclase by muscarinic receptor subtypes. Nature 334, 434–437.CrossRefGoogle ScholarPubMed
Pettit, D. A. D., Showalter, V. M., Abood, M. E. & Cabral, G. A. (1994). Expression of a cannabinoid receptor in baculovirus-infected insect cells. Biochem. Pharmacol. 48, 1231–1243.CrossRefGoogle ScholarPubMed
Peyronneau, M.-A., Renaud, J.-P., Truan, G., Urban, P., Pompon, D. & Mansuy, D. (1992). Optimisation of yeast-expressed human liver cytochrome P450 3A4 catalytic activities by coexpressing NADPH-cytochrome P450 reductase and cytochrome b5. Eur. j. Biochem. 207, 109–116.CrossRefGoogle Scholar
Pfanner, N., Hartl, F.-U. & Neupert, W. (1988). Import of proteins into mitochondria: a multi-step process. Eur. J. Biochem. 175, 205–212.CrossRefGoogle ScholarPubMed
Picot, D., Loll, P. J. & Garavito, R. M. (1994). The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature 367, 243–249.CrossRefGoogle ScholarPubMed
Pind, S., Riordan, J. R. & Williams, D. B. (1994). Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 269, 12784–12788.CrossRefGoogle ScholarPubMed
Pinner, E., Padan, E. & Schuldiner, S. (1994). Kinetic properties of NhaB, a Na+/H+ antiporter from Escherichia coli. J. Biol. Chem. 269, 26274–26279.CrossRefGoogle Scholar
Pompejus, M., Friedrich, K., Teufel, M. & Fritz, H.-J. (1993). High-yield production of bacteriorhodopsin via expression of a synthetic gene in Escherichia coli. Eur. J. Biochem. 211, 27–35.CrossRefGoogle Scholar
Pompejus, M., Hennecke, J., Althaus, T., Schmidt, B. & Fritz, H.-J. (1995). Preparation of homogeneous bacteriorhodopsin from Schizosaccharomyces pombe. FEBS Lett. Submitted.Google Scholar
Popot, J.-L. (1993). Integral membrane protein structure: transmembrane α-helices as autonomous folding domains. Curr. Opinion Struct. Biol. 3, 532–540.CrossRefGoogle Scholar
Popot, J.-L., De Vitry, C. & Atteia, A. (1994). Folding and assembly of integral membrane proteins. An introduction. In Membrane Protein Structure: Experimental Approaches, (ed. White, S. H.), Oxford: Oxford University Press pp. 41–96.CrossRefGoogle Scholar
Pos, K. M., Bott, M. & Dimroth, P. (1994). Purification of two active fusion proteins of the Na+-dependent citrate carrier of Klebsiella pneumoniae. FEBS Lett. 347, 37–41.CrossRefGoogle ScholarPubMed
Pourcher, T., Bassilana, M., Sarkar, H. K., Kaback, H. R. & Leblanc, G. (1992). Melibiose permease of Escherichia coli: Mutation of histidine-94 alters expression and stability rather than catalytic activity. Biochemistry 31, 5225–5231.CrossRefGoogle ScholarPubMed
Prange, R. & Streeck, R. E. (1995). Novel transmembrane topology of the hepatitis B virus envelope proteins. EMBO J 14, 247–256.CrossRefGoogle ScholarPubMed
Pritchett, D. B., Sontheimer, H., Gorman, C. M., Kettenmann, H., Seeburg, P. H. & Schofield, P. R. (1988). Transient expression shows ligand gating and allosteric potentiation of GABAA receptor subunits. Science 242, 1306–1308.CrossRefGoogle ScholarPubMed
Pullen, J. K., Liang, S.-M., Blake, M. S., Mates, S. & Tai, J. Y. (1995). Production of Haemophilus influenzae type-b porin in Escherichia coli and its folding into the trimeric form. Gene 152, 85–88.CrossRefGoogle ScholarPubMed
Qi, H. L., Tai, J. Y. & Blake, M. S. (1994). Expression of large amounts of Neisserial porin proteins in Escherichia coli and refolding of the proteins into native trimers. Infection and Immunity 62, 2432–2439.CrossRefGoogle ScholarPubMed
Quehenberger, O., Prossnitz, E. R., Cochrane, C. G. & Ye, R. D. (1992). Absence of G1 proteins in the Sf9 insect cell. J. Biol. Chem. 267, 19757–19760.CrossRefGoogle Scholar
Rajagopalan, S., Xu, Y. & Brenner, M. B. (1994). Retention of unassembled components of integral membrane proteins by calnexin. Science 263, 387–389.CrossRefGoogle ScholarPubMed
Raming, K., Krieger, J., Strotmann, J., Boekhoff, I., Kubick, S., Baumstark, C. & Breer, H. (1993). Cloning and expression of odorant receptors. Nature 361, 353–356.CrossRefGoogle ScholarPubMed
Rao, R. & Slayman, C. W. (1992). Mutagenesis of the yeast plasma membrane H+ATPase. Biophys. J. 62 Discussions, 228–237.CrossRefGoogle ScholarPubMed
Reiländer, H., Achilles, A., Friedel, U., Maul, G., Lottspeich, F. & Cook, N. J. (1992). Primary structure and functional expression of the Na/Ca, K-exchanger from bovine rod photoreceptors. EMBO J. 11, 1689–1695.CrossRefGoogle ScholarPubMed
Reiländer, H., Boege, F., Vasudevan, S., Maul, G., Hekman, M., Dees, C., Hampe, W., Helmreich, E. J. M. & Michel, H. (1991). Purification and functional characterization of the human β2-adrenergic receptor produced in baculovirus-infected insect cells. FEBS Lett. 282, 441–444.CrossRefGoogle Scholar
Renaud, J.-P., Cullin, C., Pompon, D., Beaune, P. & Mansuy, D. (1990). Expression of human liver cytochrome P450 IIIA4 in yeast. Eur. J. Biochem. 194, 889–896.CrossRefGoogle ScholarPubMed
Richardson, R. M. & Hosey, M. M. (1992). Agonist-induced phosphorylation and desensitization of human m2 muscarinic cholinergic receptors in Sf9 insect cells. J. Biol. Chem. 267, 22249–22255.CrossRefGoogle ScholarPubMed
Richert, N. D., Aldwin, L., Nitecki, D., Gottesman, M. M. & Pastan, I. (1988). Stability and covalent modification of P-glycoprotein in multidrug-resistant KB cells. Biochemistry 27, 7607–7613.CrossRefGoogle ScholarPubMed
Riesmeier, J. W., Willmitzer, L. & Frommer, W. B. (1992). Isolation and characterisation of a sucrose carrier cDNA from spinach by functional expression in yeast. EMBOJ. 11, 4705–4713.CrossRefGoogle ScholarPubMed
Rigaud, J.-L. & Pitard, B. (1995). Liposomes as tools for the reconstitution of biological systems. In Liposomes as tools in basic research and industry. (ed. Philipot, G.) CRC Press, Boca Raton, Florida pp. 71–88.Google Scholar
Rinken, A., Kameyama, K., Haga, T. & Engstrom, L. (1994). Solubilization of muscarinic receptor subtypes from baculovirus infected Sf9 insect cells. Biochem. Pharmacol. 48, 1245–1251.CrossRefGoogle ScholarPubMed
Rodel, J. E. & Traub, L. M. (1994). ECL detection of glycoproteins. Life Science News (Amersham International plc) 15, 2.Google Scholar
Roitelman, J., Olender, E. H., Bar-Nun, S., Dunn, W. A. Jr. & Simoni, R. D. (1992). Immunological evidence for eight spans in the membrane domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase: implications for enzyme degradation in the endoplasmic reticulum. J. Cell Biol. 117, 959–973.CrossRefGoogle Scholar
Romanos, M. A., Scorer, C. A. & Clare, J. J. (1992). Foreign gene expression in yeast: a review. Yeast 8, 423–488.CrossRefGoogle ScholarPubMed
Ross, S. M., Taverna, F. A., Pickering, D. S., Wang, L.-Y., MacDonald, J. F., Pennefather, P. S. & Hampson, D. R. (1994). Expression of functional metabotropic and ionotropic glutamate receptors in baculovirus-infected insect cells. Neurosci. Lett. 173. 139–142.CrossRefGoogle ScholarPubMed
Roth, M. G. (ED.) (1994). Protein expression in animal cells. San Diego: Academic Press.Google Scholar
Rotrosen, D., Yeung, C. L. & Katkin, J. P. (1993). Production of recombinant cytochrome b558 allows reconstitution of the phagocytic NADPH oxidase solely from recombinant proteins. J. Biol. Chem. 268, 14256–14260.CrossRefGoogle ScholarPubMed
Ruetz, S., Raymond, M. & Gros, P. (1993). Functional expression of the P-glycoprotein encoded by the mouse mdr3 gene in yeast cells. Proc. Natl. Acad. Sci. USA 90, 11588–11592.CrossRefGoogle ScholarPubMed
Sakaki, T., Oeda, K., Miyoshi, M. & Ohkawa, H. (1985). Characterisation of rat cytochrome P-450MC synthesized in Saccharomyces cerevisiae. J. Biochem. 98, 167–175.CrossRefGoogle Scholar
Sakaki, T., Oeda, K., Yabusaki, Y. & Ohkawa, H. (1986). Monooxygenase activity of Saccharomyces cerevisiae cells transformed with expression plasmids carrying rat cytochrome P-450MC cDNA. J. Biochem. 99, 741–749.CrossRefGoogle ScholarPubMed
Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989). Molecular cloning – A laboratory manual. (second edition). Cold Spring Harbor: Cold Spring Harbor Laboratory Press.Google Scholar
Sander, P., Grunewald, S., Maul, G., Reiländer, H. & Michel, H. (1994 a). Constitutive expression of the human D2s-dopamine receptor in the unicellular yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 1193, 255–262.CrossRefGoogle ScholarPubMed
Sander, P., Reiländer, H., Grünewald, S. & Michel, H. (1994 b). Expression of the human D2s dopamine receptor in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. FEBS Lett. 344, 41–46.CrossRefGoogle ScholarPubMed
Santacruz-Toloza, L., Huang, Y., John, S. A. & Papazian, D. M. (1994). Glycosylation of Shaker potassium channel protein in insect cell culture and in Xenopus oocytes. Biochemistry 33, 5607–5613.CrossRefGoogle ScholarPubMed
Sarkar, H. K., Thorens, B., Lodish, H. F. & Kaback, H. R. (1988). Expression of the human erythrocyte glucose transporter in Escherichia coli. Proc. Natl. Acad. Sci. USA 85, 5463–5467.CrossRefGoogle Scholar
Saudou, F., Boschert, U., Amlaiky, N., Plassat, J.-L. & Hen, R. (1992). A family of Drosophila serotonin receptors with distinct intracellular signalling properties and expression patterns. EMBO J. 11, 7–17.CrossRefGoogle ScholarPubMed
Sauer, N., Friedlander, K. & Graml-Wicke, U. (1990). Primary structure, genomic organisation and heterologous expression of a glucose transporter from Arabidopsis thaliana. EMBO J. 10, 3045–3050.CrossRefGoogle Scholar
Sauer, N. & Stadler, R. (1993). A sink-specific H+/monosaccharide co-transporter from Nicotinia tabacum: cloning and heterologous expression in baker's yeast. Plant J. 4, 601–610.CrossRefGoogle Scholar
Sauer, N. & Stolz, J. (1994). SUC1 and SUC2: two sucrose transporters from Arabidopsis thaliana; expression and characterization in baker's yeast and identification of the histidine tagged protein. Plant J. 6, 67–77.CrossRefGoogle ScholarPubMed
Schatz, P. J. (1993). Use of peptide libraries to map the substrate specificity of a peptide modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli. Bio/Technology 11, 1138.Google Scholar
Schertler, G. F. X. (1992). Overproduction of membrane proteins. Curr. Opinion Struct. Biol. 2, 534–544.CrossRefGoogle Scholar
Schertler, G. F. X., Bartunik, H. D., Michel, H. & Oesterhelt, D. (1993 a). Orthorhombic crystal form of bacteriorhodopsin nucleated on benzamidine diffracting to 3·6 Å resolution. J. Mol. Biol. 234, 156–164.CrossRefGoogle Scholar
Schertler, G. F. X., Villa, C. & Henderson, R. (1993 b). Projection structure of rhodopsin. Nature 362, 770–772.CrossRefGoogle ScholarPubMed
Scheuer, T., Auld, V. J., Boyd, S., Offord, J., Dunn, R. & Catterall, W. A. (1990). Functional properties of rat brain sodium channels expressed in a somatic cell line. Science 247, 854–858.CrossRefGoogle Scholar
Schiebel, E.Driessen, A. J. M., Hartl, F.-U. & Wickner, W. (1991). ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase. Cell 64, 927–939.CrossRefGoogle Scholar
Schirmer, T., Keller, T. A., Wang, Y.-F. & Rosenbusch, J. P. (1995). Structural basis for sugar translocation through maltoporin channels at 3·1 Å resolution. Science 267, 512–514.CrossRefGoogle ScholarPubMed
Schmidt, T. G. M. & Skerra, A. (1993). The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment. Prot. Eng. 6, 109–122.CrossRefGoogle ScholarPubMed
Sentenac, H., Bonneaud, N., Minet, M., Lacroute, F., Salmon, J.-M., Gaymard, F. & Grignon, C. (1992). Cloning and expression in yeast of a plant potassium ion transport system. Science 256, 663–665.CrossRefGoogle ScholarPubMed
Shand, R. F. & Betlach, M. C. (1991). Expression of the bop gene cluster of Halobacterium halobium is induced by low oxygen tension and by light. J. Bacterial. 173, 4692–4699.CrossRefGoogle ScholarPubMed
Shand, R. F., Miercke, L. J. W., Mitra, A. K., Fong, S. K., Stroud, R. M. & Betlach, M. C. (1991). Wild-type and mutant bacterioopsins D8sN, D96N, and R82Q: High-level expression in Escherichia coli. Biochemistry 30, 3082–3088.Google Scholar
Sharp, P. M. & Devine, K. M. (1989). Codon usage and gene expression level in Dictyostelium discoideum: highly expressed genes do ‘prefer’ optimal codons. Nucleic Acids Res. 17, 5029–5039.CrossRefGoogle ScholarPubMed
Shaw, G. & Kamen, R. (1986). A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 46, 659–667.CrossRefGoogle ScholarPubMed
Shimokawa, T. & Smith, W. L. (1992). Expression of prostaglandin endoperoxidase synthase-1 in a baculovirus system. Biochem. Biophys. Res. Commun. 183, 975–982.CrossRefGoogle Scholar
Shiosaki, K., Miyatsu, Y., Takahara, K., Mizokami, H., Hamada, F. & Matsubara, K. (1990). A yeast system for the stable expression of hepatitis B surface antigen. J. Biotechnol. 14, 411–422.CrossRefGoogle ScholarPubMed
Shouffani, A. & Kanner, B. I. (1990). Cholesterol is required for the reconstitution of the sodium-and chloride-coupled, γ-aminobutyric acid transporter from rat brain. J. Biol. Chem. 265, 6002–6008.CrossRefGoogle ScholarPubMed
Shuler, M. L., Wood, H. A., Granados, R. R. & Hammer, D. A. (1993). Insect cell cultures: production of improved biopesticides and proteins from recombinant DNA. New York: John Wiley & Sons.Google Scholar
Sine, S. M. & Claudio, T. (1991). Stable expression of the mouse nicotinic acetylcholine receptor in mouse fibroblasts. J. Biol. Chem. 266, 13679–13689.CrossRefGoogle ScholarPubMed
Sinning, I. (1992). Herbicide binding in the bacterial photosynthetic reaction center. Trends Biochem. Sci. 17, 150–154.CrossRefGoogle ScholarPubMed
Sinning, I. & Michel, H. (1987). Sequence analysis of mutants from Rhodopseudomonas viridis resistant to the herbicide terbutryn. Z. Naturforsch. 42c, 751–754.CrossRefGoogle Scholar
Skerjanc, I. S., Toyofuku, T., Richardson, C. & Maclennan, D. H. (1993). Mutation of glutamate 309 to glutamine alters one Ca2+-binding site in the Ca2+ATPase of sarcoplasmic reticulum expressed in Sf9 cells. J. Biol. Chem. 268, 15944–15950.CrossRefGoogle ScholarPubMed
Sleep, D., Belfield, G. P., Ballance, D. J., Steven, J., Jones, S., Evans, L. R., Moir, P. D. & Goodey, A. R. (1991). Saccharomyces cerevisiae strains that overexpress heterologous proteins. Bio/Technology 9, 183–187.Google ScholarPubMed
Smeekens, S., Weisbeek, P. & Robinson, C. (1990). Protein transport into and within chloroplasts. Trends Biochem. Sciences 15, 73–76.CrossRefGoogle ScholarPubMed
Smith, C. D., Hirayama, B. A. & Wright, E. M. (1992). Baculovirus-mediated expression of the Na+/glucose cotransporter in Sf9 cells. Biochim. Biophys. Acta 1104, 151–159.CrossRefGoogle ScholarPubMed
Smith, D. B. & Johnson, K. S. (1988). Single-step purification of polypeptides expressed in E. coli as fusions with glutathione S-transferase. Gene 67, 31–40.CrossRefGoogle Scholar
Sommer, B., Burnashev, N., Verdoorn, T. A., Keinanen, K., Sakmann, B. & Seeburg, P. H. (1992). A glutamate receptor channel with high affinity for domoate and kainate. EMBO J. 11, 1651–1656.CrossRefGoogle ScholarPubMed
Soppa, J. & Oesterhelt, D. (1989). Bacteriorhodopsin mutants of Halobacterium sp. GRB. J. Biol. Chem. 264, 13043–13048.CrossRefGoogle ScholarPubMed
Spudich, J. A. (1987). Dictyostelium discoideum: Molecular approaches to cell biology. Orlando: Academic Press.Google Scholar
Sridhar, P., Panda, A. K., Pal, R., Talwar, G. P. & Hasnain, S. E. (1993). Temporal nature of the promoter and not the relative strength determines the expression of an extensively processed protein in a baculovirus system. FEBS Lett. 315, 282–286.CrossRefGoogle ScholarPubMed
Stauffer, K. A., Kumar, N. M., Gilula, N. B. & Unwin, N. (1991). Isolation and purification of gap junction channels. J. Cell Biol. 115, 141–150.CrossRefGoogle ScholarPubMed
Studier, F. W. (1991). Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J. Mol. Biol. 219, 37–44.CrossRefGoogle ScholarPubMed
Studier, F. W., Rosenberg, A. H., Dunn, J. J. & Dubendorff, J. W. (1990). Use of T7 RNA polymerase to direct expression of cloned genes. Meth. Enzymol. 185, 60–89.CrossRefGoogle ScholarPubMed
Stults, J. T., O'Connell, K. L., Garcia, C., Wong, S., Engel, A. M., Garbers, D. L. & Lowe, D. G. (1994). The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer. Biochemistry 33, 11372–11381.CrossRefGoogle ScholarPubMed
Subramaniam, S., Gerstein, M., Oesterhelt, D. & Henderson, R. (1993). Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO J. 12, 1–8.CrossRefGoogle ScholarPubMed
Sugiyama, Y. & Mukohata, Y. (1994). Archae-opsin expressed in Escherichia coli and its conversion to purple pigment in vitro. J. Biochem. 115, 1021–1026.CrossRefGoogle Scholar
Sun, T., Naini, A. A. & Miller, C. (1994). High-level expression and functional reconstitution of Shaker K+ channels. Biochemistry 33, 9992–9999.CrossRefGoogle ScholarPubMed
Supply, P., Wach, A., Thinès-Sempoux, D. & Goffeau, A. (1993). Proliferation of intracellular structures upon overexpression of the PMA2 ATPase in Saccharomyces cerevisiae. J. Biol. Chem. 268, 19744–19752.CrossRefGoogle Scholar
Taglicht, D., Padan, E. & Schuldiner, S. (1991). Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli. J. Biol. Chem. 266, 11289–11294.CrossRefGoogle Scholar
Takeshima, H., Nishimura, S., Matsumoto, T., Ishida, H., Kangawa, K., Minamino, N., Matsuo, H., Ueda, M., Hanaoka, M., Hirose, T. & Numa, S. (1989). Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor. Nature 339, 439–445.CrossRefGoogle ScholarPubMed
Takeyasu, K., Tamkun, M. M., Renaud, K. J. & Fambrough, D. M. (1988). Ouabain-sensitive (Na+ + K+)-ATPase activity expressed in mouse L cells by transfection with DNA encoding the α-subunit of an avian sodium pump. J. Biol. Chem. 263, 4347–4354.CrossRefGoogle ScholarPubMed
Takeyasu, K., Tamkun, M. M., Siegel, N. R. & Fambrough, D. M. (1987). Expression of hybrid (Na+ + K+)-ATPase molecules after transfection of mouse Ltk− cells with DNA encoding the β-subunit of an avian brain sodium pump. J. Biol. Chem. 262, 10733–10740.CrossRefGoogle ScholarPubMed
Talbot, D., Collis, P., Antoniou, M., Vidal, M., Grosveld, F. & Greaves, D. R. (1989). A dominant control region from the human β-globin locus conferring integration site-independent gene expression. Nature 338, 352–355.CrossRefGoogle ScholarPubMed
Tate, C. G. & Blakely, R. D. (1994). The effect of N-linked glycosylation on activity of the Na+- and Cl− -dependent serotonin transporter expressed using recombinant baculovirus in insect cells. J. Biol. Chem. 269, 26303–26310.CrossRefGoogle ScholarPubMed
Taverna, F. A. & Hampson, D. R. (1994). Properties of recombinant kainate receptor expressed in baculovirus-infected insect cells. Eur.J. Pharmacol. 266, 181–186.CrossRefGoogle ScholarPubMed
Teather, R. M., Bramhall, J., Riede, I., Wright, J. K., Fürst, M., Aichele, G., Wilhelm, U. & Overath, P. (1980). Lactose carrier protein of Escherichia coli – Structure and expression of plasmids carrying the Y gene of the lac operon. Eur. J. Biochem. 108, 223–231.CrossRefGoogle Scholar
Teintze, M., Xu, Z.-J., Moffett, D. B. & Perry, B. (1994). The role of the leader sequence and its coding region in expression and assembly of bacteriorhodopsin in Halobacterium halobium. Biophys. J. 66, A43.Google Scholar
Teufel, M., Pompejus, M., Humbel, B., Friedrich, K. & Fritz, H.-J. (1993). Properties of bacteriorhodopsin derivatives constructed by insertion of an exogenous epitope into extra-membrane loops. EMBO J. 12, 3399–3408.CrossRefGoogle ScholarPubMed
Thomas, T. C. & McNamee, M. G. (1990). Purification of membrane proteins. Methods Enzymol. 182, 499–520.CrossRefGoogle ScholarPubMed
Tobias, J. W., Shrader, T. E., Rocap, G. & Varshavsky, A. (1991). The N-end rule in bacteria. Science 254, 1374–1377.CrossRefGoogle ScholarPubMed
Tordo, N., Bourhy, H., Sather, S. & Ollo, R. (1993). Structure and expression in baculovirus of the mokola virus glycoprotein: an efficient recombinant vaccine. Virology 194, 59–69.CrossRefGoogle ScholarPubMed
Toyoshima, C., Sasabe, H. & Stokes, D. L. (1993). Three-dimensional cryoelectron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane. Nature 362, 469–471.CrossRefGoogle ScholarPubMed
Truan, G., Cullin, C., Reisdorf, P., Urban, P. & Pompon, D. (1993). Enhanced in vivo monooxygenase activities of mammalian P45OS in engineered yeast cells producing high levels of NADPH-P450 reductase and human cytochrome b5. Gene 125, 49–55.CrossRefGoogle ScholarPubMed
Turcatti, G., Ceszkowski, K. & Chollet, A. (1993). Biochemical characterization and solubilization of human NK2 receptor expressed in Chinese Hamster Ovary cells. J. Receptor Res. 13, 639–652.CrossRefGoogle ScholarPubMed
Turner, B. G., Avgerinos, G. C., Melnick, L. M. & Moir, D. T. (1991). Optimisation of pro-urokinase secretion from recombinant Saccharomyces cerevisiae. Biotechnol. Bioeng. 37, 869–875.CrossRefGoogle Scholar
Tyhach, R. J., Hawrot, E., Satre, M. & Kennedy, E. P. (1979). Increased synthesis of phosphatidylserine decarboxylase in a strain of Escherichia coli bearing a hybrid plasmid. J. Biol. Chem. 254, 627–633.CrossRefGoogle Scholar
Unger, V. M. (1994). Approaches towards a high resolution structure of G protein-coupled receptors. PhD thesis, University of Cambridge, Cambridge UK.Google Scholar
Unger, V. M. & Schertler, G. F. X. (1995). Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy. Biophys. J. 68, 1776–1786.CrossRefGoogle ScholarPubMed
Unwin, N. (1993). Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol. Biol. 229, 1101–1124.CrossRefGoogle ScholarPubMed
Unwin, N. (1995). Acetylcholine receptor channel imaged in the open state. Nature 373, 37–43.CrossRefGoogle ScholarPubMed
Urban, P., Werck-Reichhart, D., Teutsch, H. G., Durst, F., Regnier, S., Kazmaier, M. & Pompon, D. (1994). Characterization of recombinant plant cinnamate 4-hydroxylase produced in yeast. Eur. J. Biochem. 222, 843–850.CrossRefGoogle ScholarPubMed
Van Weeghel, R. P., Keck, W. & Robillard, G. T. (1990). Regulated high-level expression of the mannitol permease of the phosphoenolpyruvate-dependent sugar phosphotransferase system in Escherichia coli. Proc. Natl. Acad. Sci. USA 87, 2613–2617.CrossRefGoogle Scholar
Varki, A. (1993). Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3, 97–130.CrossRefGoogle ScholarPubMed
Varshavsky, A. (1992). The N-end rule. Cell 69, 725–735.CrossRefGoogle ScholarPubMed
Vasudevan, S., Reiländer, H., Maul, G. & Michel, H. (1991). Expression and cell membrane localisation of rat m3 muscarinic acetylcholine receptor produced in Sf9 insect cells using the baculovirus system. FEBS Lett. 283, 52–56.CrossRefGoogle ScholarPubMed
Vergères, G. & Waskell, L. (1992). Expression of cytochrome b5 in yeast and characterisation of mutants of the membrane anchoring domain. J. Biol. Chem. 267, 12583–12591.CrossRefGoogle ScholarPubMed
Vergères, G., Yen, B. T. S., Aggeler, J., Lausier, J. & Waskell, L. (1993). A model system for studying membrane biogenesis – Overexpression of cytochrome b5 in yeast results in marked proliferation of the intracellular membrane. J. Cell Science 106, 249–259.CrossRefGoogle Scholar
Veyhl, M., Spangenberg, J., Puschel, B., Poppe, R., Dekel, C., Fritzsch, G., Haase, W. & Koepsell, H. (1993). Cloning of a membrane-associated protein which modifies activity and properties of the Na+-D-glucose cotransporter. J. Biol. Chem. 268, 25041–25053.CrossRefGoogle ScholarPubMed
Vialard, J., Lalumiere, M., Vernet, T., Briedis, D., Alkhatib, G., Henning, D., Levin, D. & Richardson, C. (1990). Synthesis of the membrane fusion and haemagglutinin proteins of measles virus, using a novel baculovirus vector containing the β-galactosidase gene. J. Virology 64, 37–50.CrossRefGoogle ScholarPubMed
Viitanen, P., Newman, M. J., Foster, D. L., Wilson, T. H. & Kaback, H. R. (1986). Purification, reconstitution, and characterization of the lac permease of Escherichia coli. Meth. Enzymol. 125, 429–452.Google Scholar
Villalba, J. M., Palmgren, M. G., Berberian, G. E., Ferguson, C. & Serrano, R. (1992). Functional expression of plant plasma membrane H+-ATPase in yeast endoplasmic reticulum. J. Biol. Chem 267, 12341–12349.CrossRefGoogle ScholarPubMed
Von Heijne, G. (1986). The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 5, 3021–3027.CrossRefGoogle Scholar
Von Heijne, G. (1994). Membrane proteins: From sequence to structure. Annu. Rev. Biophys. Biomol. Struct. 23, 167–192.CrossRefGoogle ScholarPubMed
Von Jagow, G. & Schägger, H. (1994). A Practical Guide to Membrane Protein Purification. San Diego, California: Academic Press.Google Scholar
Von Meyenburg, K., Jørgensen, B. B., Michelsen, O., Sørensen, L. & McCarthy, J. E. G. (1985). Proton conduction by subunit a of the membrane-bound ATP synthase of Escherichia coli revealed after induced overproduction. EMBO J. 4, 2357–2363.CrossRefGoogle ScholarPubMed
Von Meyenburg, K., Jorgensen, B. B. & Van Deurs, B. (1984). Physiological and morphological effects of overproduction of membrane-bound ATP synthase in Escherichia coli K-12. EMBO J. 3, 1791–1797.CrossRefGoogle ScholarPubMed
Waeber, U., Buhr, A., Schunk, T. & Erni, B. (1993). The glucose transporter of Escherichia coli – Purification and characterization by Ni2+ chelate affinity chromatography of the IIBCGlc subunit. FEBS Lett. 324, 109–112.CrossRefGoogle Scholar
Walker, P., Munoz, M., Combe, M.-C., Grouzmann, E., Herzog, H., Selbie, L., Shine, J., Brunner, H. R., Waeber, B. & Wittek, R. (1993). High level expression of human neuropeptide Y receptors in mammalian cells infected with a recombinant Vaccinia virus. Mol. Cell. Endocrinology 91, 107–112.CrossRefGoogle ScholarPubMed
Wathern, M. W., Aeed, P. A. & Elhammer, A. P. (1991). Characterization of oligosaccharide structures on a chimeric respiratory syncytial virus protein expressed in the insect cell line Sf9. Biochemistry 30, 2863–2868.CrossRefGoogle Scholar
Weiner, J. H., Lemire, B. D., Elmes, M. L., Bradley, R. D. & Scraba, D. G. (1984). Overproduction of fumarate reductase in Escherichia coli induces a novel intracellular lipid-protein organelle. J. Bacteriol. 158, 590–596.CrossRefGoogle ScholarPubMed
Weiner, J. H., Shaw, G., Turner, R. J. & Trieber, C. A. (1993). The topology of the anchor subunit of dimethyl sulfoxide reductase of Escherichia coli. J. Biol. Chem. 268, 3238–3244.CrossRefGoogle Scholar
Weinshank, R. L., Zgombick, J. M., Macchi, M. J., Branchek, T. A. & Hartig, P. R. (1992). Human serotonin 1D receptor is encoded by a subfamily of two distinct genes: 5-HT1Dα and 5-HT1Dβ. Proc. Natl. Acad. Set. USA 89, 3630–3634.CrossRefGoogle Scholar
Weiss, M. S., Kreusch, A., Schiltz, U., Nestel, U., Welte, W., Weckesser, J. & Schulz, G. E. (1991). The structure of porin from Rhodobacter capsulatus at 1·8 Å resolution. FEBS Lett. 280, 379–382.CrossRefGoogle ScholarPubMed
Wessels, H. P. & Spiess, M. (1988). Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence. Cell 55, 61–70.CrossRefGoogle ScholarPubMed
Wetterauer, B. W., Salger, K. & Macwilliams, H. K. (1993). Use of a transactive regulatory mutant of Dictyostelium discoideum in a eucaryotic expression system. Nucleic Acids Res. 21, 1397–1401.CrossRefGoogle Scholar
Weyer, U. & Possee, R. D. (1992). A baculovirus dual expression vector derived from the Autographa californica nuclear polyhedrosis virus polyhedrin and p10 promoters: co-expression of two influenza virus genes in insect cells. J. Gen. Virol. 72, 2967–2974.CrossRefGoogle Scholar
Whittaker, J., Okamoto, A. K., Thys, R., Bell, G. I., Steiner, D. F. & Hofmann, C. A. (1987). High-level expression of human insulin receptor cDNA in mouse NIH 3T3 cells. Proc. Natl. Acad. Sci. USA 84, 5237–5241.CrossRefGoogle ScholarPubMed
Wickner, W. (1994). How ATP drives proteins across membranes. Science 266, 1197–1198.CrossRefGoogle ScholarPubMed
Wickner, W., Driessen, A. J. M. & Hartl, F.-U. (1991). The enzymology of protein translocation across the Escherichia coli plasma membrane. Annu. Rev. Biochem. 60, 101–124.CrossRefGoogle ScholarPubMed
Wickner, W. T. & Lodish, H. F. (1985). Multiple mechanisms of protein insertion into and across membranes. Science 230, 400–407.CrossRefGoogle ScholarPubMed
Wiedmann, B., Silver, P., Schunck, W.-H. & Wiedmann, M. (1993). Overexpression of the ER-membrane protein P-450 CYP52A3 mimics sec mutant characteristics in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1153, 267–276.CrossRefGoogle Scholar
Wilkison, W. O., Walsh, J. P., Corless, J. M. & Bell, R. M. (1986). Crystalline arrays of the Escherichia coli sn-glycerol-3-phosphate acyltransferase, an integral membrane protein. J. Biol. Chem. 261, 9951–9958.CrossRefGoogle ScholarPubMed
Wilson, M. L. & MacNab, R. M. (1988). Overproduction of the MotA protein of Escherichia coli and estimation of its wild-type level. J. Bacteriol. 170, 588–597.CrossRefGoogle ScholarPubMed
Wohlrab, H. & Briggs, C. (1994). Yeast mitochondrial phosphate transport protein expressed in Escherichia coli. Site-directed mutations at threonine-43 and at a similar location in the second tandem repeat (isoleucine-141). Biochemistry 33, 9371–9375.CrossRefGoogle Scholar
Wright, K. J. & Overath, P. (1984). Purification of the lactose: H+ carrier of Escherichia coli and characterization of galactoside binding and transport. Eur. J. Biochem. 138, 497–508.CrossRefGoogle ScholarPubMed
Wu, J., Tisa, L. S. & Rosen, B. P. (1992). Membrane topology of the ArsB protein, the membrane subunit of an anion-translocating ATPase. J. Biol. Chem. 267, 12570–12576.CrossRefGoogle ScholarPubMed
Yamaguchi, A., Someya, Y. & Sawai, T. (1993). The in vivo assembly and function of the N- and C-terminal halves of the Tn10-encoded TetA protein in Escherichia coli. FEBS Lett. 324, 131–135.CrossRefGoogle Scholar
Yamashita, M., Fukui, H., Sugama, K., Horio, Y., Ito, S., Mizuguchi, H. & Wada, H. (1991). Expression cloning of a cDNA encoding the bovine histamine H1 receptor. Proc. Natl. Acad. Sci. USA 88, 11515–11519.CrossRefGoogle ScholarPubMed
Yeh, J., Seals, J. R., Murphy, C. I., Van Halbeek, H. & Cummings, R. D. (1993). Sitespecific N-glycosylation and oligosccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system. Biochemistry 32, 11087–11099.CrossRefGoogle Scholar
Yellen, G. & Migeon, J. C. (1990). Expression of Torpedo nicotinic acetylcholine receptor subunits in yeast is enhanced by use of yeast signal sequences. Gene 86, 145–152.CrossRefGoogle ScholarPubMed
Yi, C.-K., Charalambous, B. M., Emery, V. C. & Baldwin, S. A. (1992). Characterisation of functional human erythrocyte-type glucose transporter (Glut 1) expressed in insect cells using a recombinant baculovirus. Biochem. J. 283, 643–646.CrossRefGoogle Scholar
Yoon, K. L. & Guidotti, G. (1994). Studies on the membrane topology of the (Na, K)-ATPase. J. Biol. Chem. 269, 28249–28258.CrossRefGoogle ScholarPubMed
Zhang, Y. & Broome-Smith, J. K. (1990). Correct insertion of a s;.nple eukaryotic plasma-membrane protein into the cytoplasmic membrane of Escherichia coli. Gene 96, 51–57.Google Scholar
Zhu, X., Gudermann, T., Birnbaumer, M. & Birnbaumer, L. (1993). A luteinizing hormone receptor with a severely truncated cytoplasmic tail (LHR-ct628) desensitizes to the same degree as the full-length receptor. J. Biol. Chem. 268, 1723–1728.CrossRefGoogle Scholar