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Characterization of the Lysine Acylomes and the Substrates Regulated by Protein Acyltransferase in Mycobacterium smegmatis

文献类型：期刊论文

作者Xu, Jun-Yu1,2; Zhao, Lei1; Liu, XinXin1; Hu, Hao2; Liu, Ping2; Tan, Minjia2; Ye, Bang-Ce1
刊名ACS CHEMICAL BIOLOGY
出版日期2018-06
卷号13期号:6页码:1588-1597
ISSN号1554-8929
DOI10.1021/acschembio.8b00213
文献子类Article
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.
WOS关键词ACETYL-COA SYNTHETASE ; METHYLCITRATE CYCLE ; TUBERCULOSIS ; METABOLISM ; VIRULENCE ; ACYLATION ; REVEALS ; ENZYME ; CAMP ; ACETYLTRANSFERASES
资助项目National Natural Science Foundation of China[31730004] ; National Natural Science Foundation of China[21575089] ; National Natural Science Foundation of China[31670066] ; National Natural Science Foundation of China[91753203] ; Innovation Project of Instrument and Equipment Function Development of the Chinese Academy of Sciences[2060499] ; China Postdoctoral Science Foundation[2017M621567]
WOS研究方向Biochemistry & Molecular Biology
语种英语
出版者AMER CHEMICAL SOC
WOS记录号WOS:000435746200022
源URL[http://119.78.100.183/handle/2S10ELR8/279722]  
专题化学蛋白质组学研究中心
中科院受体结构与功能重点实验室
新药研究国家重点实验室
通讯作者Tan, Minjia; Ye, Bang-Ce
作者单位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
推荐引用方式
GB/T 7714		 Xu, Jun-Yu,Zhao, Lei,Liu, XinXin,et al. Characterization of the Lysine Acylomes and the Substrates Regulated by Protein Acyltransferase in Mycobacterium smegmatis[J]. ACS CHEMICAL BIOLOGY,2018,13(6):1588-1597.
APA Xu, Jun-Yu.,Zhao, Lei.,Liu, XinXin.,Hu, Hao.,Liu, Ping.,...&Ye, Bang-Ce.(2018).Characterization of the Lysine Acylomes and the Substrates Regulated by Protein Acyltransferase in Mycobacterium smegmatis.ACS CHEMICAL BIOLOGY,13(6),1588-1597.
MLA Xu, Jun-Yu,et al."Characterization of the Lysine Acylomes and the Substrates Regulated by Protein Acyltransferase in Mycobacterium smegmatis".ACS CHEMICAL BIOLOGY 13.6(2018):1588-1597.

入库方式： OAI收割

来源：上海药物研究所

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