Cross-resistance pattern to four AHAS-inhibiting herbicides of tribenuron-methyl-resistant flixweed (Descurainia sophia) conferred by Asp-376-Glu mutation in AHAS
نویسندگان
چکیده
منابع مشابه
AHAS herbicide resistance endowing mutations: effect on AHAS functionality and plant growth
Twenty-two amino acid substitutions at seven conserved amino acid residues in the acetohydroxyacid synthase (AHAS) gene have been identified to date that confer target-site resistance to AHAS-inhibiting herbicides in biotypes of field-evolved resistant weed species. However, the effect of resistance mutations on AHAS functionality and plant growth has been investigated for only a very few mutat...
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Imidazolinone herbicides, which include imazapyr, imazapic, imazethapyr, imazamox, imazamethabenz and imazaquin, control weeds by inhibiting the enzyme acetohydroxyacid synthase (AHAS), also called acetolactate synthase (ALS). AHAS is a critical enzyme for the biosynthesis of branched-chain amino acids in plants. Several variant AHAS genes conferring imidazolinone tolerance were discovered in p...
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Little seed canary grass (Phalaris minor L.) is a major weed in wheat fields in some parts of Iran. To evaluate the efficacy of molecular and greenhouse methods in detecting the resistance of 49 biotypes of canary grass(Phalaris. Spp) to acetyl-CoA carboxylase-inhibiting herbicides, two methods including whole plant screening and PCR-based molecular methods were applied. Results showed that the...
متن کاملAmino acid residues conferring herbicide resistance in tobacco acetohydroxy acid synthase.
The enzyme AHAS (acetohydroxy acid synthase), which is involved in the biosynthesis of valine, leucine and isoleucine, is the target of several classes of herbicides. A model of tobacco AHAS was generated based on the X-ray structure of yeast AHAS. Well conserved residues at the herbicide-binding site were identified, and the roles of three of these residues (Phe-205, Val-570 and Phe-577) were ...
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ژورنال
عنوان ژورنال: Journal of Integrative Agriculture
سال: 2016
ISSN: 2095-3119
DOI: 10.1016/s2095-3119(16)61432-6