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Physiological consequences of mutation for ALS-inhibitor resistance

Published online by Cambridge University Press:  12 June 2017

Charlotte V. Eberlein ,
Mary J. Guttieri ,
Philip H. Berger ,
John K. Fellman ,
Carol A. Mallory-Smith ,
Donn C. Thill ,
Roger J. Baerg  and
William R. Belknap
Mary J. Guttieri
Affiliation:
University of Idaho, Aberdeen Research and Extension Center, Aberdeen, ID 83210
Philip H. Berger
Affiliation:
University of Idaho, Moscow, ID 83844
John K. Fellman
Affiliation:
Washington State University, Pullman, WA 99164
Carol A. Mallory-Smith
Affiliation:
Oregon State University, Corvallis, OR 97331
Donn C. Thill
Affiliation:
University of Idaho, Moscow, ID 83844
Roger J. Baerg
Affiliation:
University of Idaho, Aberdeen Research and Extension Center, Aberdeen, ID 83210
William R. Belknap
Affiliation:
USDA-ARS-WRCC, Albany, CA 94706
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Abstract

Biochemical and physiological effects of target site resistance to herbicides inhibiting acetolactate synthase (ALS) were evaluated using sulfonylurea-resistant (R) and -susceptible (S) near isonuclear Lactuca sativa ‘Bibb’ lines derived by backcrossing the resistance allele from Lactuca serriola L. into L. sativa. Sequence data suggest that resistance in L. sativa is conferred by a single-point mutation that encodes a proline197 to histidine substitution in Domain A of the ALS protein; this is the same substitution observed in R L. serriola. K mapp (pyruvate) values for ALS isolated from R and S L. sativa were 7.3 and 11.1 mM, respectively, suggesting that the resistance allele did not alter the pyruvate binding domain on the ALS enzyme. Both R and S ALS had greater affinity for 2-oxobutyrate than for pyruvate at the second substrate site. Ratios of acetohydroxybutyrate: acetolactate produced by R ALS across a range of 2-oxobutyrate concentrations were similar to acetohydroxybutyrate: acetolactate ratios produced by S ALS. Specific activity of ALS from R L. sativa was 46% of the specific activity from S L. sativa, suggesting that the resistance allele has detrimental effects on enzyme function, expression, or stability. ALS activity from R plants was less sensitive to feedback inhibition by valine, leucine, and isoleucine than ALS from S plants. Valine, leucine, and isoleucine concentrations were about 1.5 times higher in R seed than in S seed on a per gram of seed basis, and concentrations of valine and leucine were 1.3 and 1.6 times higher, respectively, in R leaves than in S leaves. Findings suggest that the mutation for resistance results in altered regulation of branched-chain amino acid synthesis.

Keywords

Lactuca sativa L. ‘Bibb'Lactuca serriola L., prickly lettuce, LACSEAcetohydroxy acid synthaseacetolactate synthaseDomain A mutationsherbicide resistanceisonuclear
Type
Physiology, Chemistry, and Biochemistry
Information
Weed Science , Volume 47 , Issue 4 , August 1999 , pp. 383 - 392
Copyright
Copyright © 1999 by the Weed Science Society of America 

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References

Literature Cited

Bernasconi, P., Woodworth, A. R., Rosen, B. A., Subramanian, M. V., and Siehl, D. H. 1996. A naturally occurring point mutation confers broad range tolerance to herbicides that target acetolactate synthase. J. Biol. Chem. 270:17381–17385. [Correction J. Biol. Chem. 27:13925.]Google Scholar
Chipman, D. M., Gollop, N., Damri, B., and Barak, Z. 1990. Kinetics and mechanism of acetohydroxyacid synthases. Pages 243–267 in Barak, Z., Chipman, D. M., and Schloss, J. V., eds. Biosynthesis of Branched Chain Amino Acids. Rehovot, Israel: Balaban Publishers.Google Scholar
Delfourne, E., Bastide, J., and Genix, P. 1994. Specificity of plant acetohydroxyacid synthase: formation of products and inhibition by herbicides. Plant Physiol. Biochem. 32:473–477.Google Scholar
Dyer, W. E., Chee, P. W., and Fay, P. K. 1993. Rapid germination of sulfonylurea-resistant Kochia scoparia is associated with elevated seed levels of branched-chain amino acids. Weed Sci. 41:18–22.Google Scholar
Eberlein, C. V., Guttieri, M. J., Mallory-Smith, C. A., Thill, D. C., and Baerg, R. J. 1997. Altered acetolactatc synthase activity in ALS-inhibitor resistant prickly lettuce (Lactuca serriola). Weed Sci. 45:212–217.Google Scholar
Frohman, M. A. 1990. RACE: rapid amplification of cDNA ends. Pages 28–38 in Innis, M. A., Geland, D. H., Sninsky, J. J., White, T. J., eds. PCR Protocols: A Guide to Methods and Amplifications. San Diego: Academic Press.Google Scholar
Gollop, N., Chipman, D. M., and Barak, Z. 1983. Inhibition of acetohydroxy acid synthase by leucine. Biochim. Biophys. Acta 749:34–39.Google Scholar
Gollop, N., Damri, B., Barak, Z., and Chipman, D. 1989. Kinetics and mechanisms of acetohydroxy acid synthase isozyme III from Escherichia coli . Biochemistry 28:6310–6317.CrossRefGoogle ScholarPubMed
Guttieri, M. J., Eberlein, C. V., Mallory-Smith, C. A., and Thill, D. C. 1996. Molecular genetics of target site resistance to acetolactate synthase-inhibiting herbicides. Pages 10–16 in Brown, T. M., ed. Molecular Genetics and Ecology of Pesticide Resistance. Washington, D.C.: ACS Press.CrossRefGoogle Scholar
Guttieri, M. J., Eberlein, C. V., Mallory-Smith, C. A., Thill, D. C., and Hoffman, D. C., 1992. DNA sequence variation in Domain A of the acetolactatc synthase genes of herbicide-resistant and -susceptible weed biotypes. Weed Sci. 40:670–678.CrossRefGoogle Scholar
Guttieri, M. J., Eberlein, C. V., and Thill, D. C. 1995. Diverse mutations in the acetolactate synthase gene confer chlorsulfuron resistance in kochia (Kochia scoparia) biotypes. Weed Sci. 43:175–178.Google Scholar
Magee, P. T. and de Robichon-Szulmajster, H. 1968. The regulation of isoleucine-valine biosynthesis in Saccharomyces cerevisiae. 3. Properties and regulation of the activity of acetohydroxy-acid synthetase. Eur. J. Biochem. 3:507–511.CrossRefGoogle Scholar
Mallory-Smith, C. A. 1990. Identification and inheritance of sulfonylurea herbicide-resistance in prickly lettuce (Lactuca serriola L.). Ph.D. thesis. University of Idaho, Moscow, ID. 58 p.CrossRefGoogle Scholar
Mallory-Smith, C. A., Thill, D. C., and Dial, M. J. 1990. Identification of sulfonylurea herbicide-resistant prickly lettuce (Lactuca serriola). Weed Technol. 4:163–168.Google Scholar
Mallory-Smith, C., Thill, D. C., and Dial, M. J. 1993. ID-BR1: sulfonylurea herbicide-resistant lettuce germplasm. Hortic. Sci. 28:63–64.Google Scholar
Mazur, B. J., Chui, C.-F., and Smith, J. K. 1987. Isolation and characterization of plant genes coding for acetolactate synthase, the target enzyme for two classes of herbicides. Plant Physiol. 85:1110–1117.CrossRefGoogle ScholarPubMed
Miflin, B. J. and Cave, P. R. 1972. The control of leucine, isoleucine, and valine biosynthesis in a range of higher plants. J. Exp. Bot. 23:511–516.Google Scholar
Mourad, G., Williams, D., and King, J. 1995. A double mutant allele, csr 1–4, of Arabidopsis thaliana encodes an acetolactatc synthase with altered kinetics. Planta 196:64–68.Google Scholar
Muhitch, M. J. 1988. Acetolactate synthase activity in developing maize (Zea mays L.) kernels. Plant Physiol. 86:23–27.CrossRefGoogle ScholarPubMed
Newhouse, K., Singh, B., and Shaner, D. 1991. Mutations in corn (Zea mays L.) conferring resistance to imidazolinone herbicides. Theor. Appl. Genet. 83:65–70.Google Scholar
Newhouse, K. E., Smith, W. A., Starett, M. A., Schaefer, T. J., and Singh, B. K. 1992. Tolerance to imidazolinone herbicides in wheat. Plant Physiol. 100:882–886.Google Scholar
Rathinasabapathi, B. and King, J. 1991. Herbicide resistance in Datura innoxia . Kinetic characterization of acetolactate synthase from wild type and sulfonylurea variants. Plant Physiol. 96:255–261.Google Scholar
Rathinasabapathi, B., Williams, D., and King, J. 1990. Altered feedback sensitivity to valine, leucine, and isoleucine of acetolactate synthase from herbicide-resistant variants of Datura innoxia . Plant Sci. 67:1–6.Google Scholar
Relton, J. M., Wallsgrove, R. M., Bourgin, J. P., and Bright, S.W.J. 1986. Altered feedback sensitivity of acetohydroxyacid synthase from valineresistant mutants of tobacco (Nicotiana tabacum L.). Planta 169:46–50.Google Scholar
Rost, T. L., Gladish, D., Steffen, J., and Robbins, J. 1990. Is there a relationship between branched chain amino acid pool size and cell cycle inhibition in roots treated with imidazolinone herbicides? J. Plant Growth Regul. 9:227–232.Google Scholar
Saari, L. L., Cotterman, J. C., and Primiani, M. M. 1990. Mechanisms of sulfonylurea herbicide resistance in the broadleaf weed, Kochia scoparia . Plant Physiol. 93:55–61.CrossRefGoogle ScholarPubMed
Saari, L. L., Cotterman, J. C., Smith, W. F., and Primiani, M. M. 1992. Sulfonylurea herbicide resistance in common chickweed, perennial ryegrass, and Russian thistle. Pestic. Biochem. Physiol. 42:110–118.CrossRefGoogle Scholar
Saari, L. L., Cotterman, J. C., and Thill, D. C. 1994. Resistance to acetolactate synthase-inhibitor herbicides. Pages 83–139 in Powles, S. B. and Holtum, J.A.M., eds. Herbicide Resistance in Plants: Biology and Biochemistry. Boca Raton, FL: Lewis Publishers.Google Scholar
Schloss, J. V. 1990. Acetolactate synthase, mechanism of action and its herbicide binding site. Pestic. Sci. 29:283–292.Google Scholar
Shaner, D. L. 1991. Physiological effects of the imidazolinone herbicides. Pages 129–137 in Shaner, D. L. and O'Connor, S. L., eds. The Imidazolinone Herbicides. Boca Raton, FL: CRC Press.Google Scholar
Shaner, D. L. and Singh, B. K. 1993. Phytotoxicity of acetohydroxyacid synthase inhibitors is not due to accumulation of 2-ketobutyrate and/or 2-amino butyrate. Plant Physiol. 103:1221–1226.Google Scholar
Siehl, D. L., Bangston, A. S., Brockman, J. P., Butler, J. H., Kraatz, G. W., Lamoreaux, R. J., and Subramanian, M. V. 1996. Patterns of cross tolerance to herbicides inhibiting acetohydroxyacid synthase in commercial corn varieties designed for tolerance to imidazolinones. Crop Sci. 36:274–278.Google Scholar
Singh, B. K. and Shaner, D. L. 1995. Biosynthesis of branched chain amino acids: from test tube to field. Plant Cell 7:935–944.Google Scholar
Subramanian, M. V., Hung, H., Dias, J. M., Miner, V. W., Butler, J. H., and Jachetta, J. J. 1990. Properties of mutant acetolactate synthases resistant to triazolopyrimidine sulfonanilide. Plant Physiol. 94:239–244.CrossRefGoogle ScholarPubMed
Subramanian, M. V., Loney-Gallant, V., Dias, J. M., and Mireles, L. C. 1991. Acetolactate synthase inhibiting herbicides bind to the regulatory site. Plant Physiol. 96:310–313.CrossRefGoogle Scholar
Verwoerd, T. C., Dekker, D.M.M., and Hoekema, A. 1989. A small-scale procedure for the rapid isolation of plant RNAs. Nucl. Acids Res. 17:2362.Google Scholar