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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">An Isoleucine Residue within the Carboxyl-Transferase Domain of
Multidomain Acetyl-Coenzyme A Carboxylase Is a Major Determinant of
Sensitivity to Aryloxyphenoxypropionate But Not to Cyclohexanedione
Inhibitors<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="Chalopin, Claire" sort="Chalopin, Claire" uniqKey="Chalopin C" first="Claire" last="Chalopin">Claire Chalopin</name></author><author><name sortKey="Michel, Severine" sort="Michel, Severine" uniqKey="Michel S" first="Séverine" last="Michel">Séverine Michel</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">12857850</idno><idno type="pmc">167108</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC167108</idno><idno type="RBID">PMC:167108</idno><idno type="doi">10.1104/pp.103.021139</idno><date when="2003">2003</date><idno type="wicri:Area/Pmc/Corpus">001062</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001062</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">An Isoleucine Residue within the Carboxyl-Transferase Domain of
Multidomain Acetyl-Coenzyme A Carboxylase Is a Major Determinant of
Sensitivity to Aryloxyphenoxypropionate But Not to Cyclohexanedione
Inhibitors<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="Chalopin, Claire" sort="Chalopin, Claire" uniqKey="Chalopin C" first="Claire" last="Chalopin">Claire Chalopin</name></author><author><name sortKey="Michel, Severine" sort="Michel, Severine" uniqKey="Michel S" first="Séverine" last="Michel">Séverine Michel</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="2003">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>A 3,300-bp DNA fragment encoding the carboxyl-transferase domain of the
multidomain, chloroplastic acetyl-coenzyme A carboxylase (ACCase) was
sequenced in aryloxyphenoxypropionate (APP)-resistant and -sensitive
<italic>Alopecurus myosuroides</italic> (Huds.). No resistant plant contained an
Ile-1,781-Leu substitution, previously shown to confer resistance to APPs and
cyclohexanediones (CHDs). Instead, an Ile-2,041-Asn substitution was found in
resistant plants. Phylogenetic analysis of the sequences revealed that
Asn-2,041 ACCase alleles derived from several distinct origins.
Allele-specific polymerase chain reaction associated the presence of Asn-2,041
with seedling resistance to APPs but not to CHDs. ACCase enzyme assays
confirmed that Asn-2,041 ACCase activity was moderately resistant to CHDs but
highly resistant to APPs. Thus, the Ile-2,041-Asn substitution, which is
located outside a domain previously shown to control sensitivity to APPs and
CHDs in wheat (<italic>Triticum aestivum</italic>), is a direct cause of resistance to
APPs only. In known multidomain ACCases, the position corresponding to the
Ile/Asn-2,041 residue in <italic>A. myosuroides</italic> is occupied by an Ile or a
Val residue. In <italic>Lolium rigidum</italic> (Gaud.), we found Ile-Asn and Ile-Val
substitutions. The Ile-Val change did not confer resistance to the APP
clodinafop, whereas the Ile-Asn change did. The position and the particular
substitution at this position are of importance for sensitivity to APPs.</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>The American Society for Plant
Biologists</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">12857850</article-id><article-id pub-id-type="pmc">167108</article-id><article-id pub-id-type="publisher-id">1321716</article-id><article-id pub-id-type="doi">10.1104/pp.103.021139</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject><subj-group><subject>Whole Plant and Ecophysiology</subject></subj-group></subj-group></article-categories><title-group><article-title>An Isoleucine Residue within the Carboxyl-Transferase Domain of
Multidomain Acetyl-Coenzyme A Carboxylase Is a Major Determinant of
Sensitivity to Aryloxyphenoxypropionate But Not to Cyclohexanedione
Inhibitors<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>Chalopin</surname><given-names>Claire</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>Powles</surname><given-names>Stephen B.</given-names></name></contrib></contrib-group><aff id="N0x97f16d0.0x96a8850">Institut National de la Recherche Agronomique, Unité de Malherbologie et Agronomie, B.P. 86510, F–21065 Dijon cedex, France (C.D., C.C., S.M.); and Western Australia Herbicide Resistance Initiative, School of Plant Biology, Faculty of Natural and Agricultural Sciences, University of Western Australia, 35 Stirling Highway, 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 33–3–806–932–62.
</p></fn></author-notes><pub-date pub-type="ppub"><month>7</month><year>2003</year></pub-date><volume>132</volume><issue>3</issue><fpage>1716</fpage><lpage>1723</lpage><history><date date-type="received"><day>28</day><month>1</month><year>2003</year></date><date date-type="rev-recd"><day>17</day><month>2</month><year>2003</year></date><date date-type="accepted"><day>9</day><month>3</month><year>2003</year></date></history><copyright-statement>Copyright © 2003, The American Society for Plant
Biologists</copyright-statement><copyright-year>2003</copyright-year><abstract><p>A 3,300-bp DNA fragment encoding the carboxyl-transferase domain of the
multidomain, chloroplastic acetyl-coenzyme A carboxylase (ACCase) was
sequenced in aryloxyphenoxypropionate (APP)-resistant and -sensitive
<italic>Alopecurus myosuroides</italic> (Huds.). No resistant plant contained an
Ile-1,781-Leu substitution, previously shown to confer resistance to APPs and
cyclohexanediones (CHDs). Instead, an Ile-2,041-Asn substitution was found in
resistant plants. Phylogenetic analysis of the sequences revealed that
Asn-2,041 ACCase alleles derived from several distinct origins.
Allele-specific polymerase chain reaction associated the presence of Asn-2,041
with seedling resistance to APPs but not to CHDs. ACCase enzyme assays
confirmed that Asn-2,041 ACCase activity was moderately resistant to CHDs but
highly resistant to APPs. Thus, the Ile-2,041-Asn substitution, which is
located outside a domain previously shown to control sensitivity to APPs and
CHDs in wheat (<italic>Triticum aestivum</italic>), is a direct cause of resistance to
APPs only. In known multidomain ACCases, the position corresponding to the
Ile/Asn-2,041 residue in <italic>A. myosuroides</italic> is occupied by an Ile or a
Val residue. In <italic>Lolium rigidum</italic> (Gaud.), we found Ile-Asn and Ile-Val
substitutions. The Ile-Val change did not confer resistance to the APP
clodinafop, whereas the Ile-Asn change did. The position and the particular
substitution at this position are of importance for sensitivity to APPs.</p></abstract></article-meta><notes><fn-group><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.103.021139">www.plantphysiol.org/cgi/doi/10.1104/pp.103.021139</ext-link>.</p></fn><fn id="fn1"><label>1</label><p>This work was supported in part by the Département Santé des
Plantes et Environnement of the Institut National de la Recherche Agronomique
and by the Conseil Régional de Bourgogne (grant no. HCP
01/5112/12).</p></fn></fn-group></notes></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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