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An Ala205Val Substitution in Acetohydroxyacid Synthase of Eastern Black Nightshade (Solanum ptychanthum) Reduces Sensitivity to Herbicides and Feedback Inhibition

Published online by Cambridge University Press:  20 January 2017

Jamshid Ashigh  and
François J. Tardif
Jamshid Ashigh
Affiliation:
Department of Plant Agriculture, University of Guelph, Guelph, Ontario N1G 2W1, Canada
François J. Tardif*
Affiliation:
Department of Plant Agriculture, University of Guelph, Guelph, Ontario N1G 2W1, Canada
*
Corresponding author's E-mail: ftardif@uoguelph.ca
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Abstract

Twelve populations of eastern black nightshade from different locations in Ontario are resistant to imazethapyr. This study aimed at determining the molecular basis of resistance in these populations and the activity of the resistant acetohydroxyacid synthase (AHAS) enzyme compared to that of the sensitive AHAS in response to different herbicides and branched-chain amino acid concentration. The results of partial AHAS sequencing indicated that all resistant populations had a cytosine331 to thymine substitution coding for an alanine205 to valine substitution. In vitro AHAS enzyme assays of one resistant population showed that the specific activity of the resistant enzyme was 56% less than that of the susceptible enzyme. AHAS from the resistant population was 72-, 70-, and 64-fold less sensitive than that of the susceptible population to imazethapyr, imazamox, and primisulfuron, respectively. Furthermore, the resistant enzyme was less sensitive to feedback inhibition from branched-chain amino acids compared to the susceptible enzyme. Results confirmed that resistance in resistant populations of eastern black nightshade was conferred by target-site modification and that the Ala205Val substitution alters the kinetics and regulation of branched-chain amino acid biosynthesis.

Keywords

Imazethapyrimazamoxprimisulfuroneastern black nightshade, Solanum ptychanthum Dunal SOLPTAcetolactate synthase (ALS)point mutationbranched-chain amino acids
Type
Physiology, Chemistry, and Biochemistry
Information
Weed Science , Volume 55 , Issue 6 , December 2007 , pp. 558 - 565
Copyright
Copyright © Weed Science Society of America 

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