Multiple Mechanisms of Resistance to Fenoxaprop-P-Ethyl in United Kingdom and Other European Populations of Herbicide-Resistant Alopecurus myosuroides (Black-Grass)

Cocker, K. M.; Moss, S. R.; Coleman, J. O. D.

doi:10.1006/pest.1999.2439

Cited by 83 publications

(90 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Besides, 35 seedlings containing Asn-2,041 and/or Ile-2,041 ACCase alleles were resistant to CHDs (Table II). This was consistent with previous demonstrations that resistance to ACCase inhibitors in A. myosuroides may be due to the presence of altered target enzyme and/or to enhanced herbicide metabolization (Cocker et al, 1999;Délye et al, 2002a).…”

Section: Polymorphism Within Accase Ct Domain and Sensitivity To Appssupporting

confidence: 93%

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

et al. 2003

View full text Add to dashboard Cite

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.

show abstract

Section: Polymorphism Within Accase Ct Domain and Sensitivity To Appssupporting

confidence: 93%

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

et al. 2003

View full text Add to dashboard Cite

show abstract

“…Moreover, this work shows the possible accumulation of different resistance mechanisms in a single population and even in a single plant. This phenomena has already been observed in rye grass populations [33] and in the resistant blackgrass population from the UK, Peldon [3]. The out-crossing nature of blackgrass in combination with the extensive and varied herbicide applications provide ideal conditions for accumulation of multiple resistance mechanisms.…”

Section: Discussionmentioning

confidence: 66%

“…Thus, we may suppose that either none of the herbicide-detoxifying enzymes investigated in this study are responsible for resistance to aryloxyphenoxypropionates of the RA population, or another mechanism is involved in the resistance. A previous study, conducted with the same blackgrass population, had suggested that this population may contain a mutated acetyl CoA carboxylase (ACCAse) [3,30], the target-site of aryloxyphenoxypropionates [22,35,38,40]. Target site-based resistance is the most commonly reported mechanism of resistance to ACCaseinhibiting herbicides [9,39].…”

Section: Discussionmentioning

confidence: 99%

“…Multiple resistance is best documented in the weed species Lolium rigidum Gaud (rye grass) [4] and, to a small extent, in Alopecurus myosuroides Huds. (blackgrass), which exhibit many of the characteristics that favour the accumulation of herbicide resistance mechanisms [3]. These characteristics include a high reproductive capacity, an allogamous reproduction and a genetic plasticity [16].…”

mentioning

confidence: 99%

See 1 more Smart Citation

Enhanced activity of several herbicide-degrading enzymes: a suggested mechanism responsible for multiple resistance in blackgrass (Alopecurus myosuroides Huds.)

Letouzé

Gasquez

2003

Agronomie

View full text Add to dashboard Cite

To cite this version:Anne Letouzé, Jacques Gasquez. Enhanced activity of several herbicide-degrading enzymes: a suggested mechanism responsible for multiple resistance in blackgrass (Alopecurus myosuroides Huds. Abstract -Experiments were carried out to analyse enhanced herbicide metabolism mediated by cytochrome P450 monooxygenases (P450(s)) or glutathione-S transferases (GST(s)) as a possible mechanism responsible for multiple resistance in three blackgrass populations. The RA population is resistant to aryloxyphenoxypropionates (fops) and flupyrsulfuron, the RB to fenoxaprop-P, flupyrsulfuron and ureas and the RC to fenoxaprop-P, haloxyfop and clodinafop. Based on the coleoptile length, growth responses of seedlings to the herbicide responsible for resistance and to combined treatments of the herbicide plus P450(s) or GST(s), inhibitors were compared. Growth of the RA seedlings was significantly reduced with flupyrsulfuron plus malathion, suggesting that P450(s) activity may be involved in the resistance. In contrast, none of the four inhitors tested had an effect on the fop resistance. Fenoxaprop-P plus tridiphane, flupyrsulfuron plus malathion and ureas plus PBO or ABT significantly reduced the RB coleoptiles' growth. Therefore, multiple resistance in this population may be due to an elevation of P450(s) and GST(s) activity. In the RC population, PBO, ABT and tridiphane synergised clodinafop, haloxyfop and fenoxaprop-P effects, suggesting that the two enzymatic systems may also be involved in the RC resistances. multiple herbicide resistance / enhanced herbicide detoxification / P450(s)/GST(s) / Alopecurus myosuroides Huds.Résumé -L'amplification d'enzymes de détoxication des herbicides : un mécanisme possible responsable des résistances multiples chez le vulpin (Alopecurus myosuroides Huds.). Cette expérimentation a pour but d'analyser l'éventuelle implication de monooxygénases à cytochrome P450 (P450(s)) et de glutathione S-transférases (GST(s)) dans les résistances multiples observées chez trois populations de vulpin. La population RA résiste aux aryloxyphenoxypropionates (fops) et au flupyrsulfuron, la RB au fénoxaprop-P, au flupyrsulfuron et aux urées et la RC au fénoxaprop-P, à l'haloxyfop et au clodinafop. Les croissances de la première feuille des plantules exposées à l'herbicide seul et à un mélange "herbicide + inhibiteur" ont été analysées. La croissance des plantules RA est fortement réduite en présence de flupyrsulfuron associé au malathion. Ainsi, des P450(s) pourraient être impliquées dans la résistance de cette population. En revanche, les quatre inhibiteurs sont sans effet sur la résistance aux fops. Comparées à l'effet des herbicides utilisés seuls, les combinaisons fénoxaprop-P plus tridiphane, flupyrsulfuron plus malathion et urées plus PBO ou ABT réduisent significativement la croissance des plantules RB. Ces résultats suggèrent donc que des P450(s) et des GST(s) pourraient être responsables des résistances multiples de cette population. Pour finir, les résistances de la population RC p...

show abstract

“…FE is a postemergence aryloxyphenoxy propionate (AOPP) herbicide that is used to control annual and perennial weeds in crops, such as soybean, turf, and wheat (2,3). Many studies have demonstrated that FE can be hydrolyzed to fenoxaprop acid (FA) and further transformed into CDHB and 2-(4-hydroxyphenoxy)-propionic acid (HPP) by soil microorganisms (4)(5)(6).…”

mentioning

confidence: 99%

Metabolic Pathway Involved in 6-Chloro-2-Benzoxazolinone Degradation by Pigmentiphaga sp. Strain DL-8 and Identification of the Novel Metal-Dependent Hydrolase CbaA

Dong

Wang

Huang

et al. 2016

Appl Environ Microbiol

View full text Add to dashboard Cite

ABSTRACT6-Chloro-2-benzoxazolinone (CDHB) is a precursor of herbicide, insecticide, and fungicide synthesis and has a broad spectrum of biological activity. Pigmentiphaga sp. strain DL-8 can transform CDHB into 2-amino-5-chlorophenol (2A5CP), which it then utilizes as a carbon source for growth. The CDHB hydrolase (CbaA) was purified from strain DL-8, which can also hydrolyze 2-benzoxazolinone (BOA), 5-chloro-2-BOA, and benzamide. The specific activity of purified CbaA was 5,900 U · mg protein ؊1for CDHB, with K m and k cat values of 0.29 mM and 8,500 s ؊1 , respectively. The optimal pH for purified CbaA was 9.0, the highest activity was observed at 55°C, and the inactive metal-free enzyme could be reactivated by Mg 2؉ , Ni 2؉ , Ca 2؉ , or Zn 2؉ . Based on the results obtained for the CbaA peptide mass fingerprinting and draft genome sequence of strain DL-8, cbaA (encoding 339 amino acids) was cloned and expressed in Escherichia coli BL21(DE3). CbaA shared 18 to 21% identity with some metal-dependent hydrolases of the PF01499 family and contained the signature metal-binding motif Q 127 XXXQ 131 XD 133 XXXH 137 . The conserved amino acid residues His288 and Glu301 served as the proton donor and acceptor. E. coli BL21(DE3-pET-cbaA) resting cells could transform 0.2 mM CDHB into 2A5CP. The mutant strain DL-8⌬cbaA lost the ability to degrade CDHB but retained the ability to degrade 2A5CP, consistent with strain DL-8. These results indicated that cbaA was the key gene responsible for CDHB degradation by strain DL-8. IMPORTANCE2-Benzoxazolinone (BOA) derivatives are widely used as synthetic intermediates and are also an important group of allelochemicals acting in response to tissue damage or pathogen attack in gramineous plants. However, the degradation mechanism of BOA derivatives by microorganisms is not clear. In the present study, we reported the identification of CbaA and metabolic pathway responsible for the degradation of CDHB in Pigmentiphaga sp. DL-8. This will provide microorganism and gene resources for the bioremediation of the environmental pollution caused by BOA derivatives. 6-Chloro-2-benzoxazolinone (CDHB) is the precursor of fenoxaprop-p-ethyl (FE) and metamifop synthesis (1). FE is a postemergence aryloxyphenoxy propionate (AOPP) herbicide that is used to control annual and perennial weeds in crops, such as soybean, turf, and wheat (2, 3). Many studies have demonstrated that FE can be hydrolyzed to fenoxaprop acid (FA) and further transformed into CDHB and 2-(4-hydroxyphenoxy)-propionic acid (HPP) by soil microorganisms (4-6). Recently, the hydrolysis of FE to FA by several esterases from different microorganisms has been reported (7-9). However, the underlying genes and the metabolic pathway responsible for the degradation of CDHB in microorganisms are unknown.CDHB is a type of 2-benzoxazolinone (BOA) derivative. BOA is widely used as a synthetic intermediate of related derivatives and is an important group of allelochemicals that respond to tissue damage or pathogen attack in gramineous plants, s...

show abstract

Multiple Mechanisms of Resistance to Fenoxaprop-P-Ethyl in United Kingdom and Other European Populations of Herbicide-Resistant Alopecurus myosuroides (Black-Grass)

Cited by 83 publications

References 14 publications

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

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

Enhanced activity of several herbicide-degrading enzymes: a suggested mechanism responsible for multiple resistance in blackgrass (Alopecurus myosuroides Huds.)

Metabolic Pathway Involved in 6-Chloro-2-Benzoxazolinone Degradation by Pigmentiphaga sp. Strain DL-8 and Identification of the Novel Metal-Dependent Hydrolase CbaA

Contact Info

Product

Resources

About