文献类型：期刊文献

英文题名：Discovery of specific catalytic activity toward IAA/FA by LaSABATHs based on genome-wide phylogenetic and enzymatic analysis of SABATH gene family from Larix kaempferi

作者：Zhuge, Xiang-Lin[1] Du, Xin[1] Xiu, Zhi-Jing[1] He, Cheng-Cheng[1] Wang, Yi-Ming[1] Yang, Hai-Ling[1] Han, Xue-Min[2]

第一作者：Zhuge, Xiang-Lin

通信作者：Han, XM[1]

机构：[1]Beijing Forestry Univ, Inst Tree Dev & Genome Editing, Coll Biol Sci & Biotechnol, Natl Engn Res Ctr Tree Breeding & Ecol Restorat, Beijing 100083, Peoples R China;[2]Chinese Acad Forestry, State Key Lab Tree Genet & Breeding, Beijing 100091, Peoples R China

年份：2023

卷号：225

起止页码：1562-1574

外文期刊名：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

收录：;Scopus(收录号：2-s2.0-85143174165);WOS:【SCI-EXPANDED(收录号:WOS:000913783400001)】；

基金：Funding sources This study was supported by the National Natural Science Founda-tion of China (32071486) and the basic research funds of Chinese Academy of Forestry (No. CAFYBB2019ZY002) .

语种：英文

外文关键词：Genome-wide Larix SABATH gene family; Substrate specific and functional differentiation; Molecular docking

摘要：The SABATH methyltransferases catalyze methylation of small-molecule metabolites, which participate in plant growth, development and defense response. Given lack of genome-wide studies on gymnosperms SABATH family, the formation and functional differentiation mechanism of the Larix kaempferi SABATH gene family was systematically and exhaustively explored by analyzing gene sequence characteristics, phylogenetic relationship, expression pattern, and enzyme activities. Phylogenetic analysis showed that 247 SABATH genes from 14 land plants were divided into 4 clades, and lineage-specific gene duplication events were important factors that contributed to the evolution of the SABATH gene family in gymnosperms and angiosperms. Substrate specificity analysis of 18 Larix SABATH proteins showed that LaSABATHs could catalyze O-methylation of indole-3-acetic acid (IAA) and farnesic acid (FA), N-methylation of theobromine, and S-methylation of thiobenzoic acid. Furthermore, only LaSABATH2 and LaSABATH29 could catalyze O-methylation of FA, and only LaSABATH30 could catalyze O-methylation of IAA. Homology modeling and molecular docking studies showed the hydrogen bond formed between the His188 of LaSABATH30 and IAA and the noticeable hydrophobic IAA-binding pocket may be helpful for IAA methylation. In this study, identification of proteins with significant specific catalytic activity toward FA and IAA provided high-quality candidate genes for forest genetics and breeding.