Effects of resistance mutations of Pro197, Asp376 and Trp574 on the characteristics of acetohydroxyacid synthase (AHAS) isozymes

Yang, Qian; Deng, Wei; Wang, Shipeng; Liu, Hongjie; Li, Xuefeng; Zheng, Mingqi

doi:10.1002/ps.4889

Cited by 24 publications

(28 citation statements)

References 48 publications

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“…Mutations in genes encoding both 5-enolpyruvylshikimate-3-phosphate synthase and acetyl-CoA carboxylase (ACCase) can reduce activity of the corresponding enzymes ( Healy-Fried et al , 2007 ; Yu et al , 2007 ; Vila-Aiub et al , 2015 b ). However, the situation in ALS is more complex, with specific amino acid substitutions causing reduced, increased, or unchanged enzyme activity in different weed species ( Boutsalis et al , 1999 ; Preston et al , 2006 ; Ashigh and Tardif, 2007 ; Yu et al , 2010 ; Vercellino et al , 2018 ; Yang et al , 2018 ). A case-by-case analysis is thus required to investigate the precise impact of specific gene modifications on ALS kinetics and the fitness of resistant versus susceptible plants.…”

Section: Introductionmentioning

confidence: 99%

Unravelling the effect of two herbicide resistance mutations on acetolactate synthase kinetics and growth traits

Zhao

Yan

Du³

et al. 2020

Journal of Experimental Botany

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Gene mutations conferring herbicide resistance are hypothesized to have negative pleiotropic effects on plant growth and fitness, which may in turn determine the evolutionary dynamics of herbicide resistance alleles. We used the widespread, annual, diploid grass weed Alopecurus aequalis as a model species to investigate the effect of two resistance mutations—the rare Pro-197-Tyr mutation and the most common mutation, Trp-574-Leu—on acetolactate synthase (ALS) functionality and plant growth. We characterized the enzyme kinetics of ALS from two purified A. aequalis populations, each homozygous for the resistance mutation 197-Tyr or 574-Leu, and assessed the pleiotropic effects of these mutations on plant growth. Both mutations reduced sensitivity of ALS to ALS-inhibiting herbicides without significant changes in extractable ALS activity. The 197-Tyr mutation slightly decreased the substrate affinity (corresponding to an increased Km for pyruvate) and maximum reaction velocity (Vmax) of ALS, whereas the 574-Leu mutation significantly increased these kinetics. Significant decrease or increase in plant growth associated, respectively, with the 197-Tyr and 574-Leu resistance mutations was highly correlated with their impact on ALS kinetics, suggesting more likely persistence of the 574-Leu mutation than the 197-Tyr mutation if herbicide application is discontinued.

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Section: Introductionmentioning

confidence: 99%

Unravelling the effect of two herbicide resistance mutations on acetolactate synthase kinetics and growth traits

Zhao

Yan

Du³

et al. 2020

Journal of Experimental Botany

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“…ALS mutation diversity has been confirmed in many ALS inhibitor–resistant weeds. For example, amino acid substitution at Pro-197, Asp-376, and Trp-574 were found in D. sophia (Yang et al 2018a), kochia [ Bassia scoparia (L.) A. J. Scott] (Warwick et al 2008), and wild mustard ( Sinapis arvensis L.) (Warwick et al 2005; Whaley et al 2007); Ala-122, Pro-197, Asp-376, and Trp-574 mutations were identified in wild radish ( Raphanus raphanistrum L.) (Han et al 2012; Yu et al 2012); and Ala-122, Pro-197, Ala-205, Asp-376, Trp-574, and Ser-653 mutations were observed in redroot pigweed ( Amaranthus retroflexus L.) (Chen et al 2015; Huang et al 2016; McNaughton et al 2005). In this study, the molecular basis of ALS mutations has been well studied, and five different ALS mutations (Pro-197-Ser/Leu/His, Asp-376, and Trp-574) were established in tribenuron-methyl–resistant G. aprine .…”

Section: Resultsmentioning

confidence: 99%

Target-Site Resistance Mechanisms to Tribenuron-methyl and Cross-resistance Patterns to ALS-inhibiting Herbicides of Catchweed Bedstraw (Galium aparine) with Different ALS Mutations

Deng

Cai

et al. 2018

Weed Sci

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Catchweed bedstraw (Galium aparine L.) is a problematic dicot weed that occurs in major winter wheat (Triticum aestivum L.) fields in China. Tribenuron-methyl has been widely used to control broadleaf weeds since 1988 in China. However, overuse has led to the resistance evolution of G. aparine to tribenuron-methyl. In this study, 20 G. aparine populations collected from Shandong and Henan provinces were used to determine tribenuron-methyl resistance and target-site resistance mechanisms. In dose–response experiments, 12 G. aparine populations showed different resistance levels (2.92 to 842.41-fold) to tribenuron-methyl compared with the susceptible population. Five different acetolactate synthase (ALS) mutations (Pro-197-Leu, Pro-197-Ser, Pro-197-His, Asp-376-Glu, and Trp-574-Leu) were detected in different resistant populations. Individuals heterozygous for Pro-197-Ser and Trp-574-Leu mutations were also observed in a resistant population (HN6). In addition, pHB4 (Pro-197-Ser), pHB7 (Pro-197-His), pHB8 (Pro-197-Leu), pHB5 (Asp-376-Glu), and pHB3 (Trp-574-Leu) subpopulations individually homozygous for specific ALS mutations were generated to evaluate the cross-resistance to ALS-inhibiting herbicides. The pHB4, pHB7, pHB8, pHB5, and pHB3 subpopulations all were resistant to sulfonylurea, pyrazosulfuron-ethyl, triazolopyrimidine, flumetsulam, sulfonylamino-carbonyl-triazolinone, flucarbazone-sodium, pyrimidinyl thiobenzoate, pyribenzoxim, and the imidazolinone imazethapyr. These results indicated the diversity of the resistance-conferring ALS mutations in G. aparine, and all these mutations resulted in broad cross-resistance to five kinds of ALS-inhibiting herbicides.

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“…Several works found that specific AHAS activity, kinetic parameters and/or feedback inhibition by the branched-chain amino acids were increased, decreased, and unchanged for different amino acid substitutions. [11][12][13] A previous study in wild sunflower showed no differences between AHAS extracted from resistant and susceptible biotypes. 7 Nonetheless, the impact of mutations on AHAS activity in cultivated sunflower is still unknown.…”

Section: Introductionmentioning

confidence: 89%

“…These resistance‐conferring mutations at AHAS may cause changes on enzyme functionality and varies widely among species. Several works found that specific AHAS activity, kinetic parameters and/or feedback inhibition by the branched‐chain amino acids were increased, decreased, and unchanged for different amino acid substitutions . A previous study in wild sunflower showed no differences between AHAS extracted from resistant and susceptible biotypes .…”

Section: Introductionmentioning

confidence: 97%

Effect of Ahasl1‐1 and Ahasl1‐4 alleles on herbicide resistance and its associated dominance in sunflower

Breccia

Gianotto

Altieri³

et al. 2018

Pest Management Science

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Effects of resistance mutations of Pro197, Asp376 and Trp574 on the characteristics of acetohydroxyacid synthase (AHAS) isozymes

Cited by 24 publications

References 48 publications

Unravelling the effect of two herbicide resistance mutations on acetolactate synthase kinetics and growth traits

Unravelling the effect of two herbicide resistance mutations on acetolactate synthase kinetics and growth traits

Target-Site Resistance Mechanisms to Tribenuron-methyl and Cross-resistance Patterns to ALS-inhibiting Herbicides of Catchweed Bedstraw (Galium aparine) with Different ALS Mutations

Effect of Ahasl1‐1 and Ahasl1‐4 alleles on herbicide resistance and its associated dominance in sunflower

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