文献类型：期刊文献

英文题名：Subcellular Relocalization and Positive Selection Play Key Roles in the Retention of Duplicate Genes of Populus Class III Peroxidase Family

作者：Ren, Lin-Ling[1,2] Liu, Yan-Jing[1] Liu, Hai-Jing[1] Qian, Ting-Ting[1] Qi, Li-Wang[3] Wang, Xiao-Ru[4] Zeng, Qing-Yin[1]

第一作者：Ren, Lin-Ling

通信作者：Zeng, QY[1]

机构：[1]Chinese Acad Sci, State Key Lab Systemat & Evolutionary Bot, Inst Bot, Beijing 100093, Peoples R China;[2]Univ Chinese Acad Sci, Beijing 100049, Peoples R China;[3]Chinese Acad Forestry, Cell Biol Lab, Res Inst Forestry, Beijing 100091, Peoples R China;[4]Umea Univ, Dept Ecol & Environm Sci, UPSC, SE-90187 Umea, Sweden

年份：2014

卷号：26

期号：6

起止页码：2404-2419

外文期刊名：PLANT CELL

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000341884000008)】；

基金：We thank Chengjun Zhang of University of Chicago for assistance in branch model tests. This study was supported by grants from the Natural Science Foundation of China (NSFC 91231103 and 31330017).

语种：英文

摘要：Gene duplication is the primary source of new genes and novel functions. Over the course of evolution, many duplicate genes lose their function and are eventually removed by deletion. However, some duplicates have persisted and evolved diverse functions. A particular challenge is to understand how this diversity arises and whether positive selection plays a role. In this study, we reconstructed the evolutionary history of the class III peroxidase (PRX) genes from the Populus trichocarpa genome. PRXs are plant-specific enzymes that play important roles in cell wall metabolism and in response to biotic and abiotic stresses. We found that two large tandem-arrayed clusters of PRXs evolved from an ancestral cell wall type PRX to vacuole type, followed by tandem duplications and subsequent functional specification. Substitution models identified seven positively selected sites in the vacuole PRXs. These positively selected sites showed significant effects on the biochemical functions of the enzymes. We also found that positive selection acts more frequently on residues adjacent to, rather than directly at, a critical active site of the enzyme, and on flexible regions rather than on rigid structural elements of the protein. Our study provides new insights into the adaptive molecular evolution of plant enzyme families.