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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass<xref ref-type="fn" rid="fn1">1</xref></title><author><name sortKey="Delye, Christophe" sort="Delye, Christophe" uniqKey="Delye C" first="Christophe" last="Délye">Christophe Délye</name></author><author><name sortKey="Zhang, Xiao Qi" sort="Zhang, Xiao Qi" uniqKey="Zhang X" first="Xiao-Qi" last="Zhang">Xiao-Qi Zhang</name></author><author><name sortKey="Michel, Severine" sort="Michel, Severine" uniqKey="Michel S" first="Séverine" last="Michel">Séverine Michel</name></author><author><name sortKey="Matejicek, Annick" sort="Matejicek, Annick" uniqKey="Matejicek A" first="Annick" last="Matéjicek">Annick Matéjicek</name></author><author><name sortKey="Powles, Stephen B" sort="Powles, Stephen B" uniqKey="Powles S" first="Stephen B." last="Powles">Stephen B. Powles</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">15579665</idno><idno type="pmc">1065379</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1065379</idno><idno type="RBID">PMC:1065379</idno><idno type="doi">10.1104/pp.104.046144</idno><date when="2005">2005</date><idno type="wicri:Area/Pmc/Corpus">001048</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001048</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass<xref ref-type="fn" rid="fn1">1</xref></title><author><name sortKey="Delye, Christophe" sort="Delye, Christophe" uniqKey="Delye C" first="Christophe" last="Délye">Christophe Délye</name></author><author><name sortKey="Zhang, Xiao Qi" sort="Zhang, Xiao Qi" uniqKey="Zhang X" first="Xiao-Qi" last="Zhang">Xiao-Qi Zhang</name></author><author><name sortKey="Michel, Severine" sort="Michel, Severine" uniqKey="Michel S" first="Séverine" last="Michel">Séverine Michel</name></author><author><name sortKey="Matejicek, Annick" sort="Matejicek, Annick" uniqKey="Matejicek A" first="Annick" last="Matéjicek">Annick Matéjicek</name></author><author><name sortKey="Powles, Stephen B" sort="Powles, Stephen B" uniqKey="Powles S" first="Stephen B." last="Powles">Stephen B. Powles</name></author></analytic><series><title level="j">Plant Physiology</title><idno type="ISSN">0032-0889</idno><idno type="eISSN">1532-2548</idno><imprint><date when="2005">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>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 (<italic>Alopecurus myosuroides</italic> [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.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Plant Physiol</journal-id><journal-id journal-id-type="publisher-id">plantphysiol</journal-id><journal-title>Plant Physiology</journal-title><issn pub-type="ppub">0032-0889</issn><issn pub-type="epub">1532-2548</issn><publisher><publisher-name>American Society of Plant Biologists</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">15579665</article-id><article-id pub-id-type="pmc">1065379</article-id><article-id pub-id-type="publisher-id">046144</article-id><article-id pub-id-type="doi">10.1104/pp.104.046144</article-id><article-categories><subj-group subj-group-type="heading"><subject>Focus Issue on Abiotic Stress in Grasses</subject><subj-group><subject>Research Articles</subject></subj-group></subj-group><series-title>Focus Issue on Abiotic Stress in Grasses</series-title></article-categories><title-group><article-title>Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass<xref ref-type="fn" rid="fn1">1</xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Délye</surname><given-names>Christophe</given-names></name><xref ref-type="corresp" rid="cor1">*</xref></contrib><contrib contrib-type="author"><name><surname>Zhang</surname><given-names>Xiao-Qi</given-names></name></contrib><contrib contrib-type="author"><name><surname>Michel</surname><given-names>Séverine</given-names></name></contrib><contrib contrib-type="author"><name><surname>Matéjicek</surname><given-names>Annick</given-names></name></contrib><contrib contrib-type="author"><name><surname>Powles</surname><given-names>Stephen B.</given-names></name></contrib></contrib-group><aff id="N0x8bbdf60.0x9d059a8">Institut National de la Recherche Agronomique, Unité Mixte de Recherche, Biologie et Gestion des Adventices, F–21065 Dijon cedex, France (C.D., S.M., A.M.); and Western Australia Herbicide Resistance Initiative, School of Plant Biology, Faculty of Natural and Agricultural Sciences, University of Western Australia, Crawley, Western Australia 6009, Australia (X.-Q.Z., S.B.P.)</aff><author-notes><fn id="cor1"><label>*</label><p>Corresponding author; e-mail <email>delye@dijon.inra.fr</email>; fax 33–380–693–262.</p></fn></author-notes><pub-date pub-type="ppub"><month>3</month><year>2005</year></pub-date><volume>137</volume><issue>3</issue><fpage>794</fpage><lpage>806</lpage><history><date date-type="received"><day>11</day><month>5</month><year>2004</year></date><date date-type="rev-recd"><day>22</day><month>7</month><year>2004</year></date><date date-type="accepted"><day>17</day><month>8</month><year>2004</year></date></history><copyright-statement>Copyright © 2005, American Society of Plant Biologists</copyright-statement><copyright-year>2005</copyright-year><abstract><p>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 (<italic>Alopecurus myosuroides</italic> [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.</p></abstract></article-meta><notes><fn-group><fn id="fn1"><label>1</label><p>This work was supported by the Département Santé des Plantes et Environnement of the Institut National de la Recherche Agronomique.</p></fn><fn><p>Article, publication date, and citation information can be found at <ext-link ext-link-type="uri" xlink:href="www.plantphysiol.org/cgi/doi/10.1104/pp.104.046144">www.plantphysiol.org/cgi/doi/10.1104/pp.104.046144</ext-link>.</p></fn></fn-group></notes></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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