文献类型: 外文期刊
作者: Li, Jingbo 1 ; Peng, Qiong 1 ; Han, Heping 2 ; Nyporko, Alex 3 ; Kulynych, Tymofii 3 ; Yu, Qin 2 ; Powles, Stephen 2 ;
作者机构: 1.Hunan Acad Agr Sci, Hunan Agr Biotechnol Res Inst, Changsha 410125, Hunan, Peoples R China
2.Univ Western Australia, Sch Agr & Environm, Australian Herbicide Resistance Initiat, Perth, WA 6009, Australia
3.Taras Shevchenko Natl Univ Kyiv, UA-01033 Kiev, Ukraine
关键词: Tridax procumbens; glyphosate resistance; EPSPS mutation; polyploidy
期刊名称:JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY ( 影响因子:5.279; 五年影响因子:5.269 )
ISSN: 0021-8561
年卷期: 2018 年 66 卷 30 期
页码:
收录情况: SCI
摘要: This study confirmed the first case of glyphosate resistance in Tridax procumbens and investigated the glyphosate-resistance mechanisms. Sequencing and cloning of the full 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) coding sequences revealed a point mutation (ACC to TCC) at amino acid position 102, resulting in a novel Thr-102-Ser substitution. Other possible resistance mechanisms (i.e., target-site EPSPS-gene overexpression, nontarget-site differential glyphosate uptake and translocation) were also examined and were unlikely to be involved in resistance in this population. Structural modeling of the wild-type and mutant EPSPS in complex with glyphosate and phosphoenolpyruvate (PEP) revealed that the Thr-102-Ser substitution weakly decreased EPSPS affinity to glyphosate, but sharply increased EPSPS affinity to the natural substrate, PEP. Therefore, this novel mutation is very likely responsible for the observed glyphosate resistance in this tetraploid weed species via dual mechanisms of reducing glyphosate binding and favoring PEP binding to EPSPS.
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