Hostname: page-component-cd9895bd7-7cvxr Total loading time: 0 Render date: 2024-12-23T10:59:31.249Z Has data issue: false hasContentIssue false
  • English
  • Français

Protein disulfide isomerase in germinating wheat (Triticum aestivum) seed and during loss of viability

Published online by Cambridge University Press:  19 September 2008

M. A. Livesley ,
N. J. Bulleid  and
C. M. Bray
M. A. Livesley
Affiliation:
Department of Biochemistry and Molecular Biology, University of Manchester, Oxford Road, Manchester M13 9PT, UK
N. J. Bulleid
Affiliation:
Department of Biochemistry and Molecular Biology, University of Manchester, Oxford Road, Manchester M13 9PT, UK
C. M. Bray*
Affiliation:
Department of Biochemistry and Molecular Biology, University of Manchester, Oxford Road, Manchester M13 9PT, UK
*
* Correspondence
Get access Rights & Permissions [Opens in a new window]

Abstract

Protein disulfide isomerase (PDI E.C. 5.3.4.1) catalyses the formation of disulfide bonds in secretory or cell-surface proteins during their biosynthesis. PDI activity is associated with the microsomal fraction of the cell and has been found in several mammalian tissues and in developing wheat endosperm.

The embryo and aleurone layer of germinating seeds of the wheat cultivar Galahad showed PDI activity associated with a microsome-enriched fraction of cell homogenates PDI activity in microsome-enriched fractions from aleurone layers of normally germinating seeds was significantly higher than in their abnormally germinating counterparts and diminished as germination proceeded.

Dry embryos and germinating embryos showed less PDI activity than aleurone layers. There was no significant difference in PDI activity between microsome-enriched fractions from embryos of normally and abnormally germinating seeds at 3 or 6 days of germination.

Wheat aleurone PDI was partially purified using gel filtration and had a molecular mass of 110–130 kDa and a monomeric molecular mass of ca. 57 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis.

Keywords

aleuroneembryoprotein foldingprotein disulfide isomerasewheat
Type
Research Papers
Information
Seed Science Research , Volume 2 , Issue 2 , June 1992 , pp. 97 - 103
Copyright
Copyright © Cambridge University Press 1992

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Baulcombe, D.C., Huttly, A.K. and Martienssen, R.A. (1987) A novel wheat α-amylase gene (α-amy-3). Molecular and General Genetics 209, 33–40.CrossRefGoogle Scholar
Bewley, J.D. and Black, M. (1985) Seeds: physiology of development and germination. New York, London Plenum Press.CrossRefGoogle Scholar
Brockway, B.E. and Freedman, R.B. (1984) Protein disulphide isomerase of chick embryo tendon. Biochemical Journal 219, 51–59.CrossRefGoogle ScholarPubMed
Bulleid, N.J., Shewry, P.R. and Freedman, R.B. (in press) Exploring the structure and assembly of wheat storage proteins using an in vivo transcription/translation system. In Shewry, P.R. and Gutteridge, S. (Eds) Plant protein engineering. Cambridge University Press.Google Scholar
Bulleid, N.J. and Freedman, R.B. (1990) Cotranslational glycosylation of proteins in systems depleted of PDI. EMBO Journal 9, 3527–3532.CrossRefGoogle Scholar
Freedman, R.B. (1984) Protein disulphide isomerase. Trends in Biochemical Sciences 9, 438–441.CrossRefGoogle Scholar
Freedman, R.B., Brockway, B.E. and Lambert, N. (1984) Protein disulphide isomerase and the formation of native disulphide bonds. Biochemical Society Transactions 12, 929–932.CrossRefGoogle ScholarPubMed
Goldberger, R.F., Epstein, C.J. and Anfinsen, C.B. (1963) Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. Journal of Biological Chemistry 238, 628–635.CrossRefGoogle ScholarPubMed
Grynberg, A., Nicolas, J. and Drapron, R. (1978) Some characteristics of protein disulphide isomerases (E.C. 5.3.4.1) from wheat (Triticum vulgare) embryo. Biochimie 60, 547–551.CrossRefGoogle Scholar
Haber, E. and Anfinsen, C.B. (1962) Side chain interactions governing the pairing of half cysteine residues in ribonuclease. Journal of Biological Chemistry 237, 1839–1844.CrossRefGoogle ScholarPubMed
Holmgren, A. (1985) Thioredoxin. Annual Review of Biochemistry 54, 237–271.CrossRefGoogle ScholarPubMed
Huttly, A.K. and Baulcombe, D.C. (1990) Hormonal control of wheat α-amylase genes, pp. 171–189 in Grierson, D. and Lycett, G. (Eds) Genetic engineering of crop plants. London, Butterworths.CrossRefGoogle Scholar
Ibbetson, A.L. and Freedman, R.B. (1976) Thiol-protein disulphide oxidoreductases Biochemical Journal 159, 377–384.Google Scholar
Johnston, F.B. and Stern, H. (1957) Mass isolation of viable wheat embryos. Nature 179, 160–161.CrossRefGoogle ScholarPubMed
Koehler, S.M. and Ho, T.H.D. (1990) Hormonal regulation, processing and secretion of cysteine proteinases in barley aleurone layers. Plant Cell 2, 769–783.Google ScholarPubMed
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.CrossRefGoogle ScholarPubMed
Lambert, N. and Freedman, R.B. (1983) Structural properties of homogeneous protein disulphide isomerase from bovine liver purified by a rapid high-yielding procedure. Biochemical Journal 213, 225–234.CrossRefGoogle ScholarPubMed
Lambert, N. and Freedman, R.B. (1985) The latency of rat liver microsomal protein disulphide isomerase. Biochemical Journal 228, 635–645.CrossRefGoogle ScholarPubMed
Livesley, M.A. (1991) Protein synthesis during germination of aged wheat seed. PhD thesis, University of Manchester.Google Scholar
Livesley, M.A. and Bray, C.M. (1991) α-Amylase protein synthesis and loss of seed viability. Annals of Botany 68, 69–73.CrossRefGoogle Scholar
Lord, J.M., Kagawa, T., Moore, T.S. and Beevers, H. (1973) Endoplasmic reticulum as the site of lecithin formation in castor bean endosperm. Journal of Cell Biology 57, 659–667.CrossRefGoogle ScholarPubMed
Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) Protein measurement with the Folin reagent. Journal of Biological Chemistry 193, 265–275.CrossRefGoogle Scholar
Miflin, B.J., Burgess, S.R. and Shewry, P.R. (1981) The development of protein bodies in the storage tissues of seeds: subcellular separations of homogenates of barley, maize and wheat endosperms and of pea cotyledons. Journal of Experimental Botany 32, 199–219.CrossRefGoogle Scholar
Pihlajaniemi, T., Helaakoski, T., Tasanen, K., Myllyla, R., Huhtala, M.L., Koivu, J. and Kivirikko, K.I. (1987) Molecular cloning of the β-subunit of human prolyl-4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO Journal 6, 643–649.CrossRefGoogle ScholarPubMed
Rahmattullah, R.J., Huang, J.K., Clark, K.L., Reeck, G.R., Chandra, G.R. and Muthukrishnan, S. (1989) Nucleotide and predicted amino acid sequences of 2 different genes for high pI α-amylases from barley. Plant Molecular Biology 12, 119–121.CrossRefGoogle Scholar
Roden, L.T., Miflin, B.J. and Freedman, R.B. (1982) Protein disulphide isomerase is located in the endoplasmic reticulum of developing wheat endosperm. FEBS Letters 138, 121–124.CrossRefGoogle Scholar
Rogers, J.C. and Milliman, C. (1984) Co-ordinate increase in major transcripts from the high pI α-amylase multigene family in barley aleurone cells stimulated with gibberellic acid. Journal of Biological Chemistry 259, 12234–12240.CrossRefGoogle Scholar
Roth, R.A. and Koshland, M.E. (1981) Role of disulphide interchange enzyme in immunoglobulin synthesis. Biochemistry 20, 6594–6599.CrossRefGoogle ScholarPubMed
Schurmann, P., Gardet-Salvi, L., Kamo, M., Yano, K. and Tsugita, A. (1989) Primary structures of regulatory proteins of the ferredoxin-thioredoxin system of spinach chloroplasts. pp. 167–170 in Baltscheffsky, M. (Ed.) Current research in photosynthesis Vol. 4. Dordrecht, Kluwer Academic Publishers.Google Scholar
Simon, R., Altschuler, Y., Rubin, R. and Galili, G. (1990). Two closely related wheat storage proteins follow a markedly different subcellular route in Xenopus laevis oocytes. Plant Cell 2, 941–950.CrossRefGoogle ScholarPubMed
Sticher, L., Biswas, A.K., Bush, D.S. and Jones, R.L. (1990) Heat shock inhibits α-amylase synthesis in barley aleurone without inhibiting the activity of endoplasmic reticulum marker enzymes. Plant Physiology 92, 506–513.CrossRefGoogle ScholarPubMed
Venetianer, P. and Straub, F.B. (1963) The enzyme activation of reduced ribonuclease. Biochemica et Biophysica Acta 67, 166–168.CrossRefGoogle Scholar
Wray, W., Boulikas, T., Wray, V.P. and Hancock, R. (1981) Silver staining of proteins in polyacrylamide gels. Analytical Biochemistry 118, 197–203.CrossRefGoogle ScholarPubMed