A mutation confers Monochoria vaginalis resistance to sulfonylureas that target acetolactate synthase |
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Authors: | Guang-Xi Wang Ying Lin Misako Ito |
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Institution: | a Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan b Wuhan Institute of Botany, Chinese Academy of Sciences, Hubei 430074, China c Department of Biotechnology, South China University of Technology, Guangdong 510640, China d Department of Biology and Environmental Science, National Agricultural Research Center for Tohoku Region, Morioka 020-0198, Japan |
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Abstract: | Acetolactate synthase (ALS) is the target enzyme for four distinct families of compounds: sulfonylureas (SUs), imidazolinones, triazolopyrimidine sulfonanilides, and pyrimidinyl oxybenzoates. We cloned and sequenced the fragments encoding ALS genes from biotypes of Monochoria vaginalis susceptible (S) and resistant (R) to SU-herbicides. The nucleotide sequences of the 39 bp Domain A region for R M. vaginalis biotype differed from that of the S biotype by a single nucleotide substitution at variable Pro codon of Domain A (CCT to TCT), predicting a Pro in the S but a Ser in the R biotype. No nucleotide differences between S and R M. vaginalis were observed in Domain D. We suggest that the amino acid substitution at Domain A region is responsible for resistance to SU-herbicides in M. vaginalis collected from Ushiku City, Ibaraki Prefecture, Japan. |
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Keywords: | Acetolactate synthase Herbicide resistance Monochoria vaginalis Sulfonylurea |
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