Enhanced activity of several herbicide-degrading enzymes: 
a suggested mechanism responsible for multiple resistance 
in blackgrass (Alopecurus myosuroides Huds.)

Letouzé, Anne; Gasquez, Jacques

doi:10.1051/agro:2003036

Cited by 64 publications

(40 citation statements)

References 26 publications

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“…This was consistent with a previous demonstration that other mechanisms, such as enhanced herbicide metabolism, may also account for resistance to ACCase inhibitors in black-grass (e.g. Letouzé and Gasquez, 2003).…”

Section: Sensitivity To Apps and Chds And Amino Acid Substitutions Wisupporting

confidence: 93%

Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass

et al. 2005

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In grasses, residues homologous to residues Ile-1,781 and Ile-2,041 in the carboxyl-transferase (CT) domain of the chloroplastic acetyl-coenzyme A (CoA) carboxylase (ACCase) from the grass weed black-grass (Alopecurus myosuroides [Huds.]) are critical determinants for sensitivity to two classes of ACCase inhibitors, aryloxyphenoxypropionates (APPs) and cyclohexanediones. Using natural mutants of black-grass, we demonstrated through a molecular, biological, and biochemical approach that residues Trp-2,027, Asp-2,078, and Gly-2,096 are also involved in sensitivity to ACCase inhibitors. In addition, residues Trp-2,027 and Asp-2,078 are very likely involved in CT activity. Using three-dimensional modeling, we found that the side chains of the five residues are adjacent, located at the surface of the inside of the cavity of the CT active site, in the vicinity of the binding site for APPs. Residues 1,781 and 2,078 are involved in sensitivity to both APPs and cyclohexanediones, whereas residues 2,027, 2,041, and 2,096 are involved in sensitivity to APPs only. This suggests that the binding sites for these two classes of compounds are overlapping, although distinct. Comparison of three-dimensional models for black-grass wild-type and mutant CTs and for CTs from organisms with contrasted sensitivity to ACCase inhibitors suggested that inhibitors fitting into the cavity of the CT active site of the chloroplastic ACCase from grasses to reach their active sites may be tight. The three-dimensional shape of this cavity is thus likely of high importance for the efficacy of ACCase inhibitors.

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Section: Sensitivity To Apps and Chds And Amino Acid Substitutions Wisupporting

confidence: 93%

Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass

et al. 2005

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“…Further investigation is needed to reveal the exact underlying mechanisms. Decreased herbicide penetration/translocation and increased rates of herbicide metabolism/sequestration were found to be responsible for AHAS herbicide resistance in the case of black grass (Alopecurus myosuroides Huds) [21], rigid ryegrass (L. rigidum) [22,23], wild mustard (Sinapis arvensis L) [24] and rigid brome (bromus rigidus) [11].…”

Section: Discussionmentioning

confidence: 99%

Tribenuron-methyl resistance and mutation diversity of Pro197 in flixweed (Descurainia Sophia L.) accessions from China

Deng

Liu

Yang

et al. 2015

Pesticide Biochemistry and Physiology

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“…High frequency of herbicide resistance in Lolium rigidum P Neve and S Powles myosuroides ( Letouze and Gasquez, 2003). Glutathione transferases have also been shown to contribute to evolved herbicide resistance in A. myosuroides (Cummins et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

High survival frequencies at low herbicide use rates in populations of Lolium rigidum result in rapid evolution of herbicide resistance

2005

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The frequency of phenotypic resistance to herbicides in previously untreated weed populations and the herbicide dose applied to these populations are key determinants of the dynamics of selection for resistance. In total, 31 Lolium rigidum populations were collected from sites with no previous history of exposure to herbicides and where there was little probability of gene flow from adjacent resistant populations. The mean survival frequency across all 31 populations following two applications of commercial rates (375 g ha À1 ) of the acetyl-coenzyme A carboxylase (ACCase) inhibiting herbicide, diclofop-methyl was 0.43%. Survivors from five of these populations were grown to maturity and seed was collected. Dose-response experiments compared population level resistance to diclofop-methyl in these selected lines with their original parent populations. A single cycle of herbicide selection significantly increased resistance in all populations (LD 50 R:S ratios ranged from 2.8 to 23.2), confirming the inheritance and genetic basis of phenotypic resistance. In vitro assays of ACCase inhibition by diclofop acid indicated that resistance was due to a non-target-site mechanism. Following selection with diclofop-methyl, the five L. rigidum populations exhibited diverse patterns of crossresistance to ACCase and ALS-inhibiting herbicides, suggesting that different genes or gene combinations were responsible for resistance. The relevance of these results to the management of herbicide resistance are discussed. Heredity (2005) 95, 485-492.

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Enhanced activity of several herbicide-degrading enzymes: a suggested mechanism responsible for multiple resistance in blackgrass (Alopecurus myosuroides Huds.)

Cited by 64 publications

References 26 publications

Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass

Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass

Tribenuron-methyl resistance and mutation diversity of Pro197 in flixweed (Descurainia Sophia L.) accessions from China

High survival frequencies at low herbicide use rates in populations of Lolium rigidum result in rapid evolution of herbicide resistance

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