ArticleProceedings of the National Academy of Sciences of the United States of America1999
Herbicide sensitivity determinant of wheat plastid acetyl-CoA carboxylase is located in a 400-amino acid fragment of the carboxyltransferase domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 75 citations in OpenAlex.
- Biochemical and structural characterization of quizalofop-resistant wheat acetyl-CoA carboxylase.Scientific reports · 2022Article
- Non-target-Site Resistance inFrontiers in plant science · 2020Review
- Bacterial fatty acid metabolism in modern antibiotic discovery.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Mutations in the plastidic ACCase gene endowing resistance to ACCase-inhibiting herbicide in Phalaris minor populations from India.3 Biotech · 2016Article
- Micronucleus assay in human lymphocytes after exposure to alloxydim sodium herbicide in vitro.Cytotechnology · 2015Article
- Pantothenic acid biosynthesis in the parasite Toxoplasma gondii: a target for chemotherapy.Antimicrobial agents and chemotherapy · 2014Article
- Structure, activity, and inhibition of the Carboxyltransferase β-subunit of acetyl coenzyme A carboxylase (AccD6) from Mycobacterium tuberculosis.Antimicrobial agents and chemotherapy · 2014Article
- 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
- 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
- Fatty acid biosynthesis as a target for novel antibacterials.Current opinion in investigational drugs (London, England : 2000) · 2004Review
- 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
- An isoleucine/leucine residue in the carboxyltransferase domain of acetyl-CoA carboxylase is critical for interaction with aryloxyphenoxypropionate and cyclohexanedione inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Subcellular localization of acetyl-CoA carboxylase in the apicomplexan parasite Toxoplasma gondii.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
A series of chimeral genes, consisting of the yeast GAL10 promoter, yeast ACC1 leader, wheat acetyl-CoA carboxylase (ACCase; EC 6.4.1.2) cDNA, and yeast ACC1 3'-tail, was used to complement a yeast ACC1 mutation. These genes encode a full-length plastid enzyme, with and without the putative chloroplast transit peptide, as well as five chimeric cytosolic/plastid proteins. Four of the genes, all containing at least half of the wheat cytosolic ACCase coding region at the 5'-end, complement the yeast mutation. Aryloxyphenoxypropionate and cyclohexanedione herbicides, at concentrations below 10 microM, inhibit the growth of haploid yeast strains that express two of the chimeric ACCases. This inhibition resembles the inhibition of wheat plastid ACCase observed in vitro and in vivo. The differential response to herbicides localizes the sensitivity determinant to the third quarter of the multidomain plastid ACCase. Sequence comparisons of different multidomain and multisubunit ACCases suggest that this region includes part of the carboxyltransferase domain, and therefore that the carboxyltransferase activity of ACCase (second half-reaction) is the target of the inhibitors. The highly sensitive yeast gene-replacement strains described here provide a convenient system to study herbicide interaction with the enzyme and a powerful screening system for new inhibitors.
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