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© 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.

Abstract

EPSP synthase is the target enzyme of glyphosate herbicides. Due to the extensive use of glyphosate, it is very important to obtain EPSPS genes with high glyphosate resistance for the development of transgenic crops. GR79-EPSPS is a class I EPSP synthase with certain glyphosate resistance isolated from glyphosate-contaminated soil. After more than 1000 generations, a Y40I substitution was identified, and the enzyme had a nearly 1.8-fold decrease in Km [PEP] and a 1.7-fold increase in Ki[glyphosate] compared to the wild-type enzyme. Enzyme dynamics and molecular dynamics analysis showed that the substitution was near the hinge region of EPSPS, and the affinity of glyphosate binding to amino acid residues of the active site decreased due to Y40I substitution, resulting in an increase in glyphosate resistance. These results provide more evidence for the combination of directed evolution and rational design of protein engineering.

Details

Title
A Highly Glyphosate-Resistant EPSPS Mutant from Laboratory Evolution
Author
Yuan, Yuan 1 ; Zhou, Zhengfu 2 ; Zhan, Yuhua 2 ; Ke, Xiubin 2 ; Yan, Yongliang 2   VIAFID ORCID Logo  ; Lin, Min 2 ; Li, Pengcheng 2 ; Jiang, Shijie 1 ; Wang, Jin 3 ; Lu, Wei 2 

 School of Life Science and Engineering, Southwest University of Science and Technology, Mianyang 621010, China; [email protected] (Y.Y.); [email protected] (S.J.) 
 Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China; [email protected] (Z.Z.); [email protected] (Y.Z.); [email protected] (X.K.); [email protected] (Y.Y.); [email protected] (M.L.); [email protected] (P.L.) 
 School of Life Science and Engineering, Southwest University of Science and Technology, Mianyang 621010, China; [email protected] (Y.Y.); [email protected] (S.J.); Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China; [email protected] (Z.Z.); [email protected] (Y.Z.); [email protected] (X.K.); [email protected] (Y.Y.); [email protected] (M.L.); [email protected] (P.L.) 
First page
5723
Publication year
2022
Publication date
2022
Publisher
MDPI AG
e-ISSN
20763417
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
2674337821
Copyright
© 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.