Improvement of Glyphosate Resistance through Concurrent Mutations in Three Amino Acids of the Pantoea sp. 5-Enolpyruvylshikimate-3- Phosphate Synthase | Zendy

Feng Liu | Zendy; Yueping Cao | Zendy

Open Access

Improvement of Glyphosate Resistance through Concurrent Mutations in Three Amino Acids of the Pantoea sp. 5-Enolpyruvylshikimate-3- Phosphate Synthase

Author(s) -

Feng Liu,

Yueping Cao

Publication year - 2018

Publication title -

journal of microbiology and biotechnology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.601

H-Index - 64

eISSN - 1738-8872

pISSN - 1017-7825

DOI - 10.4014/jmb.1801.01026

Subject(s) - shikimate pathway , mutant , glyphosate , shikimic acid , biology , mutagenesis , biochemistry , amino acid , transgene , arabidopsis , enzyme , aromatic amino acids , gene , microbiology and biotechnology

Glyphosate inhibits the target enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) in the shikimate pathway. A mutant of EPSPS from Pantoea sp. was identified using site-directed mutagenesis (SDM). The mutant significantly improved glyphosate resistance. The mutant had mutations in three amino acids: Gly97 to Ala, Thr 98 to Ile and Pro 102 to Ser. These mutation sites in E.coli have been studied as significant active sites of glyphosate resistance. However, in our research they were found to jointly contribute to the improvement of glyphosate tolerance. In addition, the level of glyphosate tolerance in transgenic Arabidopsis confirmed the potentiality of the mutant in breeding glyphosate-resistant plants.

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