ArticlePlant physiology2005
Molecular bases for sensitivity to acetyl-coenzyme A carboxylase inhibitors in black-grass.
Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 204 citations in OpenAlex.
- Asp-2078-Gly mutation confers ACCase-inhibiting herbicide resistance in Leptochloa chinensis (L.) Nees.Pest management science · 2026Article
- Genome Editing Enhanced Abiotic Stress ToleranceIn Cereal Crops.Functional & integrative genomics · 2025Review
- Herbicide resistance inFrontiers in plant science · 2025Article
- Target-site mutations Ile1781Leu and Ile2041Asn in thePlant direct · 2024Article
- Overexpression ofPlant signaling & behavior · 2023Article
- Standing genetic variation fuels rapid evolution of herbicide resistance in blackgrass.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mechanism of metamifop resistance inFrontiers in plant science · 2023Article
- Effects of the Rhizosphere FungusInternational journal of molecular sciences · 2022Article
- Article
- Point Mutations and Cytochrome P450 Can Contribute to Resistance to ACCase-Inhibiting Herbicides in ThreePlants (Basel, Switzerland) · 2021Article
- Resistance Mechanism to Metsulfuron-Methyl inPlants (Basel, Switzerland) · 2021Article
- The Development of Herbicide Resistance Crop Plants Using CRISPR/Cas9-Mediated Gene Editing.Genes · 2021Review
- Molecular characteristics of the first case of haloxyfop-resistant Poa annua.Scientific reports · 2020Article
- Target-Site Mutations Conferring Herbicide Resistance.Plants (Basel, Switzerland) · 2019Review
- Fitness costs associated with acetyl-coenzyme A carboxylase mutations endowing herbicide resistance in American sloughgrass (Ecology and evolution · 2019Article
- Resistance determination of the ACCase-inhibiting herbicide of clodinafop propargyl in Avena ludoviciana (Durieu), and study of their interaction using molecular docking and simulation.Molecular biology reports · 2019Article
- Herbicidal Activity and Molecular Docking Study of Novel ACCase Inhibitors.Frontiers in plant science · 2018Article
- Synonymous mutation gene design to overexpress ACCase in creeping bentgrass to obtain resistance to ACCase-inhibiting herbicides.Transgenic research · 2016Article
- Mutations in the plastidic ACCase gene endowing resistance to ACCase-inhibiting herbicide in Phalaris minor populations from India.3 Biotech · 2016Article
- Multiple Herbicide Resistance in Lolium multiflorum and Identification of Conserved Regulatory Elements of Herbicide Resistance Genes.Frontiers in plant science · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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