Cross‐resistance patterns to ACCase‐inhibiting herbicides conferred by mutant ACCase isoforms in <i>Alopecurus myosuroides</i> Huds. (black‐grass), re‐examined at the recommended herbicide field rate

Délye, Christophe; Matéjicek, Annick; Michel, Séverine

doi:10.1002/ps.1614

Cited by 81 publications

(94 citation statements)

References 20 publications

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“…Resistance mutations have not been observed for either of these two residues, probably because such mutations will also lead to a significant loss in catalytic activity of the enzyme. (17)(18)(19)(20). Of these, the D2078G and C2088R mutations confer resistance to both FOPs and DIMs, and the I1781L mutation confers resistance to FOPs and some DIMs.…”

Section: Resultsmentioning

confidence: 99%

Mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by pinoxaden

Kim

Tong

2010

Proc. Natl. Acad. Sci. U.S.A.

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Acetyl-CoA carboxylases (ACCs) are crucial metabolic enzymes and have been targeted for drug development against obesity, diabetes, and other diseases. The carboxyltransferase (CT) domain of this enzyme is the site of action for three different classes of herbicides, as represented by haloxyfop, tepraloxydim, and pinoxaden. Our earlier studies have demonstrated that haloxyfop and tepraloxydim bind in the CT active site at the interface of its dimer. However, the two compounds probe distinct regions of the dimer interface, sharing primarily only two common anchoring points of interaction with the enzyme. We report here the crystal structure of the CT domain of yeast ACC in complex with pinoxaden at 2.8-Å resolution. Despite their chemical diversity, pinoxaden has a similar binding mode as tepraloxydim and requires a small conformational change in the dimer interface for binding. Crystal structures of the CT domain in complex with all three classes of herbicides confirm the importance of the two anchoring points for herbicide binding. The structures also provide a foundation for understanding the molecular basis of the herbicide resistance mutations and cross resistance among the herbicides, as well as for the design and development of new inhibitors against plant and human ACCs.fatty acid metabolism | metabolic syndrome | structure-based drug design

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Section: Resultsmentioning

confidence: 99%

Mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by pinoxaden

Kim

Tong

2010

Proc. Natl. Acad. Sci. U.S.A.

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“…ACCase-inhibitors [8,14,22,23], and the homo/heterozygous status of the plants for the mutation can also influence the resistance levels [6,14]. In general, among the common mutant ACCase alleles, 1781Leu, 2078Gly and 2088Arg mutant alleles can confer resistance to APPs, CHDs and pinoxaden [2,24,25]; 2027Cys and 2041Asn alleles can cause resistance to APPs and pinoxaden, but not to CHDs [6,10,24]; 2096Ala allele confers resistance mainly to APPs [14].…”

Section: Commercialmentioning

confidence: 97%

Cross-resistance patterns to ACCase-inhibitors in American sloughgrass (Beckmannia syzigachne Steud.) homozygous for specific ACCase mutations

Liu

Yuan

et al. 2016

Pesticide Biochemistry and Physiology

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“…Thus, it is our conclusion that a R. cochinchinensis population from Costa Rica has evolved resistance to fluazifop-P-butyl and the mechanism of resistance is based on an altered target site conferred by the Trp-2027-Cys mutation. Furthermore, since the Trp-2027-Cys mutation is known to confer resistance to all APPs herbicides while having small effects on the CHDs and DENs (Liu et al, 2007;Délye et al, 2008;Jang et al, 2013), our recommendation is that Costa Rican farmers should avoid the use of other members of the APPs group (e.g., fenoxaprop, haloxyfop and clodinafop), but they could still control APPs-resistant itchgrass populations using CHDs and DENs herbicides. Further studies are needed to verify this, since the same population could harbor individuals with different point mutations conferring resistance to ACCase herbicides from different groups, or individual plants could carry two different mutant sites that endow resistance to more than one ACCase herbicide group.…”

Section: Resultsmentioning

confidence: 99%

Molecular Basis for Resistance to Fluazifop-P-Butyl in Itchgrass (Rottboellia cochinchinensis) from Costa Rica

Castillo-Matamoros¹,

Brenes-Angulo²,

Murillo

et al. 2016

Planta daninha

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Rottboellia cochinchinensis is an annual grass weed species known as itchgrass, or "caminadora" in America´s Spanish speaking countries, and has become a major and troublesome weed in several crops. The application of fluazifop-P-butyl at recommended rates (125 g a.i. ha-1) was observed to be failing to control itchgrass in a field in San José, Upala county, Alajuela province, Costa Rica. Plants from the putative resistant R. cochinchinensis population survived fluazifop-P-butyl when treated with 250 g a.i. ha-1 (2X label rate) at the three- to four-leaf stage under greenhouse conditions. PCR amplification and sequencing of partial carboxyl transferase domain (CT) of the acetyl-CoA carboxylase (ACCase) gene were used to determine the molecular mechanism of resistance. A single non-synonymous point mutation from TGG (susceptible plants) to TGC (putative resistant plants) that leads to a Trp-2027-Cys substitution was found. This Trp-2027-Cys mutation is known to confer resistance to all aryloxyphenoxyproprionate (APP) herbicides to which fluazifop-P-butyl belongs. To the best of our knowledge, this is the first report of fluazifop-P-butyl resistance and a mutation at position 2027 for a Costa Rican R. cochinchinensis population.

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Cross‐resistance patterns to ACCase‐inhibiting herbicides conferred by mutant ACCase isoforms in Alopecurus myosuroides Huds. (black‐grass), re‐examined at the recommended herbicide field rate

Cited by 81 publications

References 20 publications

Mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by pinoxaden

Mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by pinoxaden

Cross-resistance patterns to ACCase-inhibitors in American sloughgrass (Beckmannia syzigachne Steud.) homozygous for specific ACCase mutations

Molecular Basis for Resistance to Fluazifop-P-Butyl in Itchgrass (Rottboellia cochinchinensis) from Costa Rica

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