Acetolactate synthase mutation conferring imidazolinone-specific herbicide resistance in Amaranthus hybridus

Research output: Contribution to journalArticle

Abstract

Acetolactate synthase (ALS) catalyzes the first common step in the biosynthesis of branched-chain amino acids in plants and is the target of several herbicides. ALS inhibitors have enjoyed popularity as herbicides due to numerous attributes, although their current adequacy in weed control programs is hampered by herbicide resistance. Most cases of ALS-inhibitor resistance have resulted from selection of an altered target site. The study herein reports on an alanine by threonine amino acid substitution at position 122 of ALS as the basis for imidazolinone-specific resistance in an A. hybridus population from Illinois. In vitro inhibition of enzymatic activity (I50) required 1000-fold greater concentration of imazethapyr in the resistant population compared with a susceptible control. This mutation represents the second ALS alteration associated with herbicide resistance in a natural A. hybridus population.

Original languageEnglish (US)
Pages (from-to)475-479
Number of pages5
JournalJournal of Plant Physiology
Volume163
Issue number4
DOIs
StatePublished - Feb 22 2006

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Acetolactate Synthase
Herbicide Resistance
Amaranthus
Amaranthus hybridus
acetolactate synthase
herbicide resistance
mutation
Mutation
Herbicides
herbicides
Weed Control
Population
Branched Chain Amino Acids
imazethapyr
branched chain amino acids
amino acid substitution
Threonine
Amino Acid Substitution
threonine
Alanine

Keywords

  • ALS
  • Imazethapyr
  • Smooth pigweed

ASJC Scopus subject areas

  • Physiology
  • Agronomy and Crop Science
  • Plant Science

Cite this

Acetolactate synthase mutation conferring imidazolinone-specific herbicide resistance in Amaranthus hybridus. / Trucco, Federico; Hager, Aaron G; Tranel, Patrick J.

In: Journal of Plant Physiology, Vol. 163, No. 4, 22.02.2006, p. 475-479.

Research output: Contribution to journalArticle

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