Acetyl-CoA carboxylase overexpression in herbicide-resistant large crabgrass (Digitaria sanguinalis)

Martin Laforest; Brahim Soufiane; Marie-Josée Simard; Kristen Obeid; Eric Page; Robert E Nurse

doi:10.1002/ps.4675

Acetyl-CoA carboxylase overexpression in herbicide-resistant large crabgrass (Digitaria sanguinalis)

Pest Management Science ◽

10.1002/ps.4675 ◽

2017 ◽

Vol 73 (11) ◽

pp. 2227-2235 ◽

Cited By ~ 32

Author(s):

Martin Laforest ◽

Brahim Soufiane ◽

Marie-Josée Simard ◽

Kristen Obeid ◽

Eric Page ◽

...

Keyword(s):

Acetyl Coa Carboxylase ◽

Digitaria Sanguinalis ◽

Acetyl Coa ◽

Herbicide Resistant ◽

Large Crabgrass

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Physiological Basis for Antagonism of Fluazifop-P by DPX-PE350

Weed Science ◽

10.1017/s0043174500081042 ◽

1995 ◽

Vol 43 (2) ◽

pp. 184-191 ◽

Cited By ~ 23

Author(s):

Kenneth L. Ferreira ◽

James D. Burton ◽

Harold D. Coble

Keyword(s):

Enzyme Assay ◽

Protein Extraction ◽

Herbicidal Activity ◽

Acetyl Coa Carboxylase ◽

Acetyl Coa ◽

Carboxylase Activity ◽

Physiological Basis ◽

Treated Leaf ◽

Large Crabgrass

Greenhouse and laboratory experiments were conducted to determine the effect of DPX-PE350 on the herbicidal activity of fluazifop-P on large crabgrass. Greenhouse experiments indicated that fluazifop-P activity was antagonized by DPX-PE350. This antagonism was reduced by increasing fluazifop-P rates or by applying DPX-PE350 after fluazifop-P. Applying DPX-PE350 24 h prior to fluazifop-P reduced fluazifop-P activity more than applying it 10 min prior. The effect of DPX-PE350 application to large crabgrass on extractable acetyl-CoA carboxylase activity, and the effect of DPX-PE350 on acetyl-CoA carboxylase activity in vitro also was studied. Applying DPX-PE350 to large crabgrass prior to protein extraction did not reduce fluazifop-P inhibition of acetyl CoA carboxylase activity in vitro. The presence of DPX-PE350 in the enzyme assay mix did not affect fluazifop-P inhibition of acetyl-CoA carboxylase activity. The effect of DPX-PE350 on uptake, translocation, and metabolism of fluazifop-P was considered. DPX-PE350 did not affect uptake of fluazifop-P by large crabgrass. Applying DPX-PE350 24 h prior to fluazifop-P decreased translocation of fluazifop-P out of the treated leaf 44 to 53% whereas mixing DPX-PE350 with fluazifop-P decreased fluazifop-P translocation only 15 to 17%. Metabolism of fluazifop-P was not affected by applications of DPX-PE350. These studies suggest that the antagonism of fluazifop-P activity by DPX-PE350 is due to decreased translocation of fluazifop-P out of the treated leaf.

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An isoleucine to leucine mutation in acetyl-CoA carboxylase confers herbicide resistance in wild oat

Genome ◽

10.1139/g02-080 ◽

2002 ◽

Vol 45 (6) ◽

pp. 1049-1056 ◽

Cited By ~ 51

Author(s):

Michael J Christoffers ◽

Michelle L Berg ◽

Calvin G Messersmith

Keyword(s):

Herbicide Resistance ◽

Dna Sequences ◽

Resistance Mutation ◽

Triticum Aestivum L ◽

Wild Oat ◽

Acetyl Coa Carboxylase ◽

Acetyl Coa ◽

Herbicide Resistant ◽

Binding Domains ◽

Substitution Site

Wild oat (Avena fatua L.) populations resistant to herbicides that inhibit acetyl-CoA carboxylase (ACCase; EC 6.4.1.2) represent an increasingly important weed control problem. The objective of this study was to determine the ACCase mutation responsible for herbicide resistance in a well-studied wild oat biotype (UM1). A 2039-bp region encompassing the carboxybiotin and acetyl-CoA binding domains of multifunctional plastidic ACCase was analyzed. DNA sequences representing three plastidic ACCase gene loci were isolated from both the resistant UM1 and a herbicide-susceptible biotype, consistent with the hexaploid nature of wild oat. Only one nonsynonymous point mutation was found among the resistant wild oat sequences, inferring an isoleucine to leucine substitution. The position of this substitution corresponds to residue 1769 of wheat (Triticum aestivum L.) plastidic ACCase (GenBank accession No. AF029895). Analysis of an F2 population derived from a cross between a herbicide-resistant and a susceptible biotype confirmed co-segregation of herbicide resistance with the mutated ACCase. We conclude that the isoleucine to leucine mutation is responsible for herbicide resistance in UM1 wild oat based on a comparison of the substitution site across species and ACCase types. While isoleucine is conserved among plastidic ACCases of herbicide-susceptible grasses, leucine is found in plastidic and cytosolic forms of multifunctional herbicide-resistant ACCase.Key words: acetyl-CoA carboxylase, herbicide resistance, mutation, wild oat.

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