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Plant Physiology 132:1716-1723 (2003)
© 2003 American Society of Plant Biologists

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WHOLE PLANT AND ECOPHYSIOLOGY

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 Inhibitors1

Christophe Délye*, Xiao-Qi Zhang, Claire Chalopin, Séverine Michel and Stephen B. Powles

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.)

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 Alopecurus myosuroides (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 (Triticum aestivum), is a direct cause of resistance to APPs only. In known multidomain ACCases, the position corresponding to the Ile/Asn-2,041 residue in A. myosuroides is occupied by an Ile or a Val residue. In Lolium rigidum (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.


Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.103.021139.

1 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).

* Corresponding author; e-mail delye{at}dijon.inra.fr; fax 33–3–806–932–62.

Received January 28, 2003; returned for revision February 17, 2003; accepted March 9, 2003.




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