Properties of acetolactate synthase from sulfonylurea-resistant Scirpus juncoides Roxb. var. ohwianus T. Koyama

Tanaka, Yasushi

doi:10.1016/j.pestbp.2003.07.005

Cited by 27 publications

(26 citation statements)

References 20 publications

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“…These results are in agreement with the location of the mutations, not at the active site but within the substrate‐access channel . Moreover, AHAS kinetic studies with sunflower and several other species have shown similar Km app values for resistant and susceptible genotypes …”

Section: Discussionsupporting

confidence: 85%

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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Section: Discussionsupporting

confidence: 85%

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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“…One SU‐susceptible accession was collected from a paddy field in Kyoto Prefecture. Tanaka () reported that this accession was susceptible to imazosulfuron. The characteristics of these accessions and geographic collection sites are shown in Table and Figure , respectively.…”

Section: Methodsmentioning

confidence: 98%

Characterization of acetolactate synthase from sulfonylurea herbicide‐resistant Schoenoplectus juncoides

Yamato

Sada

Ikeda

2013

Weed Biology and Management

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Ten accessions of sulfonylurea‐resistant Schoenoplectus juncoides were collected from paddy fields in Japan. In order to characterize acetolactate synthase from sulfonylurea‐resistant S. juncoides, acetolactate synthase amino acid substitutions, whole‐plant growth inhibition and acetolactate synthase enzyme inhibition were examined. Schoenoplectus juncoides has two acetolactate synthase genes (ALS1 and ALS2). The sulfonylurea‐resistant accessions harbored amino acid substitutions at Pro197 or Trp574 in either ALS1 or ALS2 (the amino acid number is standardized to the Arabidopsis thaliana sequence). The whole plants of all the sulfonylurea‐resistant accessions showed resistance to imazosulfuron. The resistance level depended on the altered amino acid residues in acetolactate synthase. The acetolactate synthase enzyme that was partially purified from all the sulfonylurea‐resistant accessions was less sensitive to imazosulfuron, compared to the susceptible accession, suggesting that the resistance is related to the altered acetolactate synthase enzyme. In addition, the concentration–response inhibition of acetolactate synthase activity by imazosulfuron in the sulfonylurea‐resistant accessions was remarkably different with the presence of an amino acid substitution in either ALS1 or ALS2. Furthermore, the concentration–response inhibition of acetolactate synthase activity in the sulfonylurea‐resistant accessions with a P197S, P197T or W574L mutation showed a double‐sigmoid curve. The regression analysis of enzyme inhibition suggested that the abundance ratio of ALS1 to ALS2 enzymes was approximately 70:30%, with a range of ±15%. Taken together, these results suggest that the resistance of sulfonylurea‐resistant accessions of S. juncoides is related to altered acetolactate synthase in either ALS1 or ALS2, although the abundance of the altered acetolactate synthase in the plants is different among the sulfonylurea‐resistant accessions.

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“…Research conducted with ALS of E. heterophyla (Vargas et al, 1999), Lactuta serriola (Eberlein et al, 1997) and Scirpus juncoides (Tanaka, 2003) showed similar results, in which the kinetics of the enzyme of the biotype resistant to the inhibiting herbicide of ALS was not altered.…”

Section: Differencesmentioning

confidence: 87%

Differential susceptibility of biotypes of conyza sumatrensis to Chlorimuron-ethyl herbicide

et al. 2014

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-Horseweed (Conyza spp.) is an annual weed, infesting soybean crops in southern Brazil, with chlorimuron-ethyl being one of the most commonly used herbicides for its control. However, in recent soybean harvests, an unsatisfactory control of this weed using this herbicide was observed, generating suspicion regarding the selection of resistant biotypes. The objective of this study was to evaluate the susceptibility of horseweed biotypes to the herbicide chlorimuron-ethyl. Two experiments were conducted in a greenhouse; in the first one, the biotypes were selected selected, and the second experiment was arranged in a 5 x 5 factorial in a completely randomized design with four replications. The treatments used in the preparation of the dose response curves were doses of the herbicide chlorimuron-ethyl (0.0, 1.56, 3.13, 6.25, 12.5, and 25 g ha -1 ), applied on the five horseweed biotypes at the 3-4 leaf growth stage. The variables evaluated were visual control percentage and shoot dry weight, compared to the control without herbicide application, and plant acetolactate accumulation. It was concluded that there is a differential susceptibility among the biotypes at doses of less than 20 g ha -1 (dose response curves), which indicates low-level resistance. The practical consequences are the indications of chlorimuron-ethyl application at the maximum doses recomended and that the practice of rotating mechanisms of action must be used in the chemical weed management of these areas.Keywords: chemical control, horseweed, low level resistance, ALS. chlorimuron-ethyl (0,0, 1,56, 3,13, 6,25, 12,5 RESUMO -A buva (Conyza spp.) é uma planta daninha anual que infesta lavouras de soja na região

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Properties of acetolactate synthase from sulfonylurea-resistant Scirpus juncoides Roxb. var. ohwianus T. Koyama

Cited by 27 publications

References 20 publications

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

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

Characterization of acetolactate synthase from sulfonylurea herbicide‐resistant Schoenoplectus juncoides

Differential susceptibility of biotypes of conyza sumatrensis to Chlorimuron-ethyl herbicide

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