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Acetolactate synthase mutation conferring imidazolinone-specific herbicide resistance in Amaranthus hybridus.
- Source :
-
Journal of plant physiology [J Plant Physiol] 2006 Mar; Vol. 163 (4), pp. 475-9. Date of Electronic Publication: 2005 Sep 12. - Publication Year :
- 2006
-
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 (I(50)) 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.
- Subjects :
- Acetolactate Synthase antagonists & inhibitors
Amaranthus drug effects
Amaranthus enzymology
Amino Acid Sequence
Drug Resistance
Herbicides antagonists & inhibitors
Illinois
Kinetics
Molecular Sequence Data
Sequence Alignment
Sequence Analysis, Protein
Acetolactate Synthase genetics
Amaranthus genetics
Enzyme Inhibitors pharmacology
Herbicides pharmacology
Mutation
Subjects
Details
- Language :
- English
- ISSN :
- 0176-1617
- Volume :
- 163
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Journal of plant physiology
- Publication Type :
- Academic Journal
- Accession number :
- 16455361
- Full Text :
- https://doi.org/10.1016/j.jplph.2005.06.015