文献类型：期刊文献

英文题名：Functional and structural profiles of GST gene family from three Populus species reveal the sequence-function decoupling of orthologous genes

作者：Yang, Qi[1,2,3] Han, Xue-Min[2] Gu, Jin-Ke[4] Liu, Yan-Jing[1,2] Yang, Mao-Jun[4] Zeng, Qing-Yin[1,2,3]

第一作者：Yang, Qi

通信作者：Zeng, QY[1];Zeng, QY[2];Zeng, QY[3]

机构：[1]Chinese Acad Forestry, State Key Lab Tree Genet & Breeding, Beijing 100091, Peoples R China;[2]Chinese Acad Sci, Inst Bot, State Key Lab Systemat & Evolutionary Bot, Beijing 100093, Peoples R China;[3]Univ Chinese Acad Sci, Beijing 100049, Peoples R China;[4]Tsinghua Univ, Sch Life Sci, Tsinghua Peking Ctr Life Sci, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China

年份：2019

卷号：221

期号：2

起止页码：1060-1073

外文期刊名：NEW PHYTOLOGIST

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000453883200044)】；

基金：We thank the three anonymous reviewers for valuable comments and suggestions that helped to improve the manuscript. This study was supported by the National Science Fund for Distinguished Young Scholars (31425006) and the Chinese Academy of Forestry (CAFYBB2018ZX001). We would like to thank the staff at beamline BL17U of the Shanghai Synchrotron Radiation Facility for their assistance with data collection.

语种：英文

外文关键词：functional divergence; glutathione S-transferase (GST); orthologous gene; Populus; protein function

摘要：A common assumption in comparative genomics is that orthologous genes are functionally more similar than paralogous genes. However, the validity of this assumption needs to be assessed using robust experimental data. We conducted tissue-specific gene expression and protein function analyses of orthologous groups within the glutathione S-transferase (GST) gene family in three closely related Populus species: Populus trichocarpa, Populus euphratica and Populus yatungensis. This study identified 21 GST orthologous groups in the three Populus species. Although the sequences of the GST orthologous groups were highly conserved, the divergence in enzymatic functions was prevalent. Through site-directed mutagenesis of orthologous proteins, this study revealed that nonsynonymous substitutions at key amino acid sites played an important role in the divergence of enzymatic functions. In particular, a single amino acid mutation (Arg39 -> Trp39) contributed to P. euphratica PeGSTU30 possessing high enzymatic activity via increasing the hydrophobicity of the active cavity. This study provided experimental evidence showing that orthologues belonging to the gene family have functional divergences. The nonsynonymous substitutions at a few amino acid sites resulted in functional divergence of the orthologous genes. Our findings provide new insights into the evolution of orthologous genes in closely related species.