Acetylome Analysis Reveals Diverse Functions of Lysine Acetylation in Mycobacterium tuberculosis
Liu, Fengying1; Yang, Mingkun2; Wang, Xude1; Yang, Shanshan1; Gu, Jing1; Zhou, Jie3; Zhang, Xian-En4; Deng, Jiaoyu1; Ge, Feng2
2014-12-01
Source PublicationMOLECULAR & CELLULAR PROTEOMICS
ISSN1535-9476
Volume13Issue:12Pages:3352-3366
AbstractThe lysine acetylation of proteins is a reversible post-translational modification that plays a critical regulatory role in both eukaryotes and prokaryotes. Mycobacterium tuberculosis is a facultative intracellular pathogen and the causative agent of tuberculosis. Increasing evidence shows that lysine acetylation may play an important role in the pathogenesis of M. tuberculosis. However, only a few acetylated proteins of M. tuberculosis are known, presenting a major obstacle to understanding the functional roles of reversible lysine acetylation in this pathogen. We performed a global acetylome analysis of M. tuberculosis H37Ra by combining protein/peptide prefractionation, antibody enrichment, and LC-MS/MS. In total, we identified 226 acetylation sites in 137 proteins of M. tuberculosis H37Ra. The identified acetylated proteins were functionally categorized into an interaction map and shown to be involved in various biological processes. Consistent with previous reports, a large proportion of the acetylation sites were present on proteins involved in glycolysis/gluconeogenesis, the citrate cycle, and fatty acid metabolism. A NAD(+)-dependent deacetylase (MRA_1161) deletion mutant of M. tuberculosis H37Ra was constructed and its characterization showed a different colony morphology, reduced biofilm formation, and increased tolerance of heat stress. Interestingly, lysine acetylation was found, for the first time, to block the immunogenicity of a peptide derived from a known immunogen, HspX, suggesting that lysine acetylation plays a regulatory role in immunogenicity. Our data provide the first global survey of lysine acetylation in M. tuberculosis. The dataset should be an important resource for the functional analysis of lysine acetylation in M. tuberculosis and facilitate the clarification of the entire metabolic networks of this life-threatening pathogen.
SubtypeArticle
KeywordTandem Mass-spectrometry Bacterium Bacillus-subtilis M-bovis Bcg Escherichia-coli Coa Synthetase Saccharomyces-cerevisiae Phosphoproteome Analysis Protein Identification Reversible Acetylation Plasmodium-falciparum
DOI10.1074/mcp.M114.041962
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
Indexed BySCI
Language英语
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemical Research Methods
WOS KeywordTANDEM MASS-SPECTROMETRY ; BACTERIUM BACILLUS-SUBTILIS ; M-BOVIS BCG ; ESCHERICHIA-COLI ; COA SYNTHETASE ; SACCHAROMYCES-CEREVISIAE ; PHOSPHOPROTEOME ANALYSIS ; PROTEIN IDENTIFICATION ; REVERSIBLE ACETYLATION ; PLASMODIUM-FALCIPARUM
WOS IDWOS:000345626400011
Citation statistics
Cited Times:75[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/20372
Collection藻类生物学及应用研究中心_水生生物分子与细胞生物学研究中心
Affiliation1.Chinese Acad Sci, Wuhan Inst Virol, Wuhan 430071, Peoples R China
2.Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China
3.Foshan Fourth Peoples Hosp, Foshan, Peoples R China
4.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
Recommended Citation
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Liu, Fengying,Yang, Mingkun,Wang, Xude,et al. Acetylome Analysis Reveals Diverse Functions of Lysine Acetylation in Mycobacterium tuberculosis[J]. MOLECULAR & CELLULAR PROTEOMICS,2014,13(12):3352-3366.
APA Liu, Fengying.,Yang, Mingkun.,Wang, Xude.,Yang, Shanshan.,Gu, Jing.,...&Ge, Feng.(2014).Acetylome Analysis Reveals Diverse Functions of Lysine Acetylation in Mycobacterium tuberculosis.MOLECULAR & CELLULAR PROTEOMICS,13(12),3352-3366.
MLA Liu, Fengying,et al."Acetylome Analysis Reveals Diverse Functions of Lysine Acetylation in Mycobacterium tuberculosis".MOLECULAR & CELLULAR PROTEOMICS 13.12(2014):3352-3366.
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