Systematic Proteomic Analysis of Protein Methylation in Prokaryotes and Eukaryotes Revealed Distinct Substrate Specificity
Zhang, Min2,3,4; Xu, Jun-Yu1,2,3; Hu, Hao2,3; Ye, Bang-Ce1; Tan, Minjia2,3,4
刊名PROTEOMICS
2018-01
卷号18期号:1
关键词heavy methyl silac histone mass spectrometry methylation proteomics
ISSN号1615-9853
DOI10.1002/pmic.201700300
文献子类Article
英文摘要The studies of protein methylation mainly focus on lysine and arginine residues due to their diverse roles in essential cellular processes from gene expression to signal transduction. Nevertheless, atypical protein methylation occurring on amino acid residues, such as glutamine and glutamic acid, is largely neglected until recently. In addition, the systematic analysis for the distribution of methylation on different amino acids in various species is still lacking, which hinders our understanding of its functional roles. In this study, we deeply explored the methylated sites in three species Escherichia coli, Saccharomyces cerevisiae, and HeLa cells by employing MS-based proteomic approach coupled with heavy methyl SILAC method. We identify a total of 234 methylated sites on 187 proteins with high localization confidence, including 94 unreported methylated sites on nine different amino acid residues. KEGG and gene ontology analysis show the pathways enriched with methylated proteins are mainly involved in central metabolism for E. coli and S. cerevisiae, but related to spliceosome for HeLa cells. The analysis of methylation preference on different amino acids is conducted in three species. Protein N-terminal methylation is dominant in E. coli while methylated lysines and arginines are widely identified in S. cerevisiae and HeLa cells, respectively. To study whether some atypical protein methylation has biological relevance in the pathological process in mammalian cells, we focus on histone methylation in diet-induced obese (DIO) mouse. Two glutamate methylation sites showed statistical significance in DIO mice compared with chow-fed mice, suggesting their potential roles in diabetes and obesity. Together, these findings expanded the methylome database from microbes to mammals, which will benefit our further appreciation for the protein methylation as well as its possible functions on disease.
资助项目National Basic Research Program of China (973 Program)[2014CBA02004] ; Natural Science Foundation of China[31670066] ; Innovation Project of Instrument and Equipment Function Development of the Chinese Academy of Sciences[2060499] ; Special Project on Precision Medicine under the National Key RD Program[SQ2017YFSF090210] ; Personalized Medicines-Molecular Signature-based Drug Discovery and Development[00000000] ; Strategic Priority Research Program of the Chinese Academy of Sciences[XDA12020325] ; National Natural Science Foundation of China[31730004]
WOS关键词ARGININE METHYLATION ; SACCHAROMYCES-CEREVISIAE ; LYSINE METHYLATION ; ESCHERICHIA-COLI ; BACTERIAL CHEMOTAXIS ; S-ADENOSYLMETHIONINE ; IN-VIVO ; GLOBAL ANALYSIS ; RELEASE FACTORS ; METHYLTRANSFERASE
WOS研究方向Biochemistry & Molecular Biology
语种英语
出版者WILEY
WOS记录号WOS:000419942500005
内容类型期刊论文
源URL[http://119.78.100.183/handle/2S10ELR8/272345]  
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Ye, Bang-Ce; Tan, Minjia
作者单位1.East China Univ Sci & Technol, Lab Biosyst & Microanal, State Key Lab Bioreactor Engn, Shanghai, Peoples R China
2.Chinese Acad Sci, Chem Prote Ctr, Shanghai Inst Mat Med, Shanghai, Peoples R China;
3.Chinese Acad Sci, State Key Lab Drug Res, Shanghai Inst Mat Med, Shanghai, Peoples R China;
4.Univ Chinese Acad Sci, Beijing, Peoples R China;
推荐引用方式
GB/T 7714
Zhang, Min,Xu, Jun-Yu,Hu, Hao,et al. Systematic Proteomic Analysis of Protein Methylation in Prokaryotes and Eukaryotes Revealed Distinct Substrate Specificity[J]. PROTEOMICS,2018,18(1).
APA Zhang, Min,Xu, Jun-Yu,Hu, Hao,Ye, Bang-Ce,&Tan, Minjia.(2018).Systematic Proteomic Analysis of Protein Methylation in Prokaryotes and Eukaryotes Revealed Distinct Substrate Specificity.PROTEOMICS,18(1).
MLA Zhang, Min,et al."Systematic Proteomic Analysis of Protein Methylation in Prokaryotes and Eukaryotes Revealed Distinct Substrate Specificity".PROTEOMICS 18.1(2018).
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