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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. Kmapp (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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