文献类型：期刊文献

英文题名：Characterization of the Lysine Acylomes and the Substrates Regulated by Protein Acyltransferase in Mycobacterium smegmatis

作者：Xu, Jun-Yu[1,2];Zhao, Lei[1];Liu, XinXin[1];Hu, Hao[2];Liu, Ping[2];Tan, Minjia[2];Ye, Bang-Ce[1]

机构：[1]East China Univ Sci & Technol, Lab Biosyst & Microanal, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China

年份：2018

卷号：13

期号：6

起止页码：1588

外文期刊名：ACS CHEMICAL BIOLOGY

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000435746200022)】；

基金：This work was supported by grants from the National Natural Science Foundation of China (31730004, 21575089) (to B.C.Y.), (31670066, 91753203) (to M.T.), the Innovation Project of Instrument and Equipment Function Development of the Chinese Academy of Sciences (2060499) (to M.T.), and China Postdoctoral Science Foundation (2017M621567) (to J.Y.X.).

语种：英文

摘要：Protein acylation plays important roles in bacterial pathogenesis through regulation of enzymatic activity, protein stability, nucleic acid binding ability, and protein-protein interactions. Mycobacteria, a genus including invasive pathogens known to cause serious diseases, shapes its pathogenicity through adaptation of its energy metabolism to microenvironments encountered within mammalian hosts. In this process, acetyl-CoA and propionyl-CoA function as important intermediates. However, the function of acetyl-CoA/propionyl-CoA driven protein acylation remains to be elucidated. Herein, we systematically investigated protein acetylome/propionylome in the nonpathogenic Mycobacterium smegmatis through antibody-enrichment-based proteomic analysis in which 146 acetylated sites on 121 proteins and 26 propionylated sites on 25 proteins were identified. After that, characteristic differences of the two acylomes were elucidated through such bioinformatic methods as motif analysis, protein-protein analysis, Gene Ontology analysis, and KEGG analysis. In addition, quantitative mass spectrometric method was used to evaluate the site-specific and motif-biased catalytic mechanism mediated by the cAMP-dependent acetyltransferase MsKat in M. smegmatis. Furthermore, we raised the possibility that both O-serine and N-epsilon-lysine acetylation might coregulate the propionyl-CoA synthetase. This study described the landscape of acetylome and propionylome in the M. smegmatis, showing an unexpected role of protein acylation regulation in mycobacteria.