Artículo
A122S, A205V, D376E, W574L and S653N substitutions in acetolactate synthase (ALS) from Amaranthus palmeri show different functional impacts on herbicide resistance
Fecha de publicación:
02/2022
Editorial:
John Wiley & Sons Ltd
Revista:
Pest Management Science
ISSN:
1526-498X
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
BACKGROUND: Amaranthus palmeri S. Watson, a problematic weed infesting summer crops in Argentina, has developed multiple herbicide resistance. Resistance to acetolactate synthase (ALS)-inhibiting herbicides is particularly common, with high-level resistance mostly caused by different mutations in the ALS enzyme. Six versions of the enzyme were identified from a resistant A. palmeri population, carrying substitutions D376E, A205V, A122S, A282D, W574L and S653N. This work aims to provide a comparative analysis of these mutants and the wild-type (WT) enzyme to fully understand the herbicide resistance. Thus, all the versions of the ALS gene from A. palmeri were heterologously expressed and purified to evaluate their kinetics and inhibitory response against imazethapyr, diclosulam, chlorimuron-ethyl, flucarbazone-sodium and bispyribac-sodium. RESULTS: A decrease in catalytic efficiency was detected in the A205V, A122S–A282D, W574L and S653N ApALS enzymes, whereas only A205V and W574L substitutions also produced a decrease in the substrate affinity. In vitro ALS inhibition assays confirmed cross-resistance to almost all the herbicides tested, with the exception of A282D ApALS, which was as susceptible as WT ApALS. Moreover, the results confirmed that the novel substitution A122S provides cross-resistance to at least one herbicide within each of the five families of ALS inhibitors, and this property could be explained by a lower number of hydrophobic interactions between the herbicides and the mutant enzyme. CONCLUSION: This is the first report to compare various mutations in vitro from A. palmeri ALS. Our data contribute to understanding the impacts of herbicide resistance in this species. © 2021 Society of Chemical Industry.
Palabras clave:
Herbicide resistance
,
Amaranthus palmeri
,
Mutants
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Articulos(CEFOBI)
Articulos de CENTRO DE EST.FOTOSINTETICOS Y BIOQUIMICOS (I)
Articulos de CENTRO DE EST.FOTOSINTETICOS Y BIOQUIMICOS (I)
Citación
Palmieri, Valeria Esther; Alvarez, Clarisa Ester; Permingeat, Hugo Raúl; Perotti, Valeria Elisa; A122S, A205V, D376E, W574L and S653N substitutions in acetolactate synthase (ALS) from Amaranthus palmeri show different functional impacts on herbicide resistance; John Wiley & Sons Ltd; Pest Management Science; 78; 2; 2-2022; 749-757
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