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A naturally evolved mutation (Ser59Gly) in glutamine synthetase confers glufosinate resistance in plants

文献类型： 外文期刊

作者： Zhang, Chun 1 ; Yu, Qin 2 ; Han, Heping 2 ; Yu, Chaojie 1 ; Nyporko, Alex 3 ; Tian, Xingshan 1 ; Beckie, Hugh 2 ; Powles, Stephen 2 ;

作者机构： 1.Guangdong Acad Agr Sci, Inst Plant Protect, Guangdong Prov Key Lab High Technol Plant Protect, Guangzhou 510640, Peoples R China

2.Univ Western Australia, Sch Agr & Environm, Australian Herbicide Resistance Initiat, Crawley, WA 6009, Australia

3.Taras Shevchenko Natl Univ Kyiv, Kiev, Ukraine

关键词： Eleusine indica; glufosinate; glutamine synthetase; target site mutation

期刊名称：JOURNAL OF EXPERIMENTAL BOTANY （ 影响因子：7.298； 五年影响因子：8.291 ）

ISSN： 0022-0957

年卷期： 2022 年 73 卷 7 期

页码：

收录情况： SCI

摘要： This work reveals a naturally evolving point mutation in glutamine synthetase that confers resistance to glufosinate in the globally important C(4)weed species Eleusine indica. Glufosinate is an important and widely used non-selective herbicide active on a wide range of plant species. Evolution of resistance to glufosinate in weedy plant species (including the global weed Eleusine indica) is underway. Here, we established the molecular basis of target site glufosinate resistance in Eleusine indica. Full-length E. indica glutamine synthetase (GS) iso-genes (EiGS1-1, 1-2, 1-3, and EiGS2) were cloned, and expression of EiGS1-1 and EiGS1-2 was higher than that of EiGS2. A novel point mutation resulting in a Ser59Gly substitution in EiGS1-1 was identified in glufosinate-resistant plants. Rice calli and seedlings transformed with the mutant EiGS1-1 gene were resistant to glufosinate. Purified mutant EiGS1-1 expressed in yeast was more tolerant to glufosinate than the wild-type variant. These transgenic results correlate with a more glufosinate-resistant GS in the crude tissue extract of resistant versus susceptible E. indica plants. Structural modelling of the mutant EiGS1-1 revealed that Ser59 is not directly involved in glufosinate binding but is in contact with some important binding residues (e.g. Glu297) and especially with Asp56 that forms an intratoroidal contact interface. Importantly, the same Ser59Gly mutation was also found in geographically isolated glufosinate-resistant populations from Malaysia and China, suggesting parallel evolution of this resistance mutation.

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