ArticleProceedings of the National Academy of Sciences of the United States of America2001
An isoleucine/leucine residue in the carboxyltransferase domain of acetyl-CoA carboxylase is critical for interaction with aryloxyphenoxypropionate and cyclohexanedione inhibitors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 148 citations in OpenAlex.
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- Repeated evolution of herbicide resistance inEvolutionary applications · 2023Article
- Target-Site Mutations Conferring Herbicide Resistance.Plants (Basel, Switzerland) · 2019Review
- 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
- Article
- Purification and cellular localization of the Entamoeba histolytica transcarboxylase.Parasitology research · 2012Article
- Trypanosoma brucei: inhibition of acetyl-CoA carboxylase by haloxyfop.Experimental parasitology · 2012Article
- Recombinant yeast screen for new inhibitors of human acetyl-CoA carboxylase 2 identifies potential drugs to treat obesity.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- A different mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by tepraloxydim.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Nanomolecular HLA-DR10 antibody mimics: A potent system for molecular targeted therapy and imaging.Cancer biotherapy & radiopharmaceuticals · 2008Article
- Diversity of acetyl-coenzyme A carboxylase mutations in resistant Lolium populations: evaluation using clethodim.Plant physiology · 2007Article
- Single-site mutations in the carboxyltransferase domain of plastid acetyl-CoA carboxylase confer resistance to grass-specific herbicides.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Article
- Recurrent selection with reduced herbicide rates results in the rapid evolution of herbicide resistance in Lolium rigidum.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2005Article
- Molecular bases for sensitivity to acetyl-coenzyme A carboxylase inhibitors in black-grass.Plant physiology · 2005Article
- Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Complex nested promoters control tissue-specific expression of acetyl-CoA carboxylase genes in wheat.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Graminicide insensitivity correlates with herbicide-binding co-operativity on acetyl-CoA carboxylase isoforms.The Biochemical journal · 2003Article
- Article
- Expression of cytosolic and plastid acetyl-coenzyme A carboxylase genes in young wheat plants.Plant physiology · 2003Article
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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
cDNA fragments encoding the carboxyltransferase domain of the multidomain plastid acetyl-CoA carboxylase (ACCase) from herbicide-resistant maize and from herbicide-sensitive and herbicide-resistant Lolium rigidum were cloned and sequenced. A Leu residue was found in ACCases from herbicide-resistant plants at a position occupied by Ile in all ACCases from sensitive grasses studied so far. Leu is present at the equivalent position in herbicide-resistant ACCases from other eukaryotes. Chimeric ACCases containing a 1000-aa fragment of two ACCase isozymes found in a herbicide-resistant maize were expressed in a yeast ACC1 null mutant to test herbicide sensitivity of the enzyme in vivo and in vitro. One of the enzymes was resistant/tolerant, and one was sensitive to haloxyfop and sethoxydim, rendering the gene-replacement yeast strains resistant and sensitive to these compounds, respectively. The sensitive enzyme has an Ile residue, and the resistant one has a Leu residue at the putative herbicide-binding site. Additionally, a single Ile to Leu replacement at an equivalent position changes the wheat plastid ACCase from sensitive to resistant. The effect of the opposite substitution, Leu to Ile, makes Toxoplasma gondii apicoplast ACCase resistant to haloxyfop and clodinafop. In this case, inhibition of the carboxyltransferase activity of ACCase (second half-reaction) of a large fragment of the Toxoplasma enzyme expressed in Escherichia coli was tested. The critical amino acid residue is located close to a highly conserved motif of the carboxyltransferase domain, which is probably a part of the enzyme active site, providing the basis for the activity of fop and dim herbicides.
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