Comprehensive profiling of lysine acetylome in Staphylococcus aureus

作     者：ZHANG Yi WU ZhiXiang WAN XueLian LIU Ping ZHANG JiBao YE Yang ZHAO YingMing TAN MinJia 

作者机构：Chemical Proteomics Center & State Key Laboratory of Drug ResearchShanghai Institute of Materia MedicaChinese Academy of Sciences Natural Products Chemistry Department & State Key Laboratory of Drug ResearchShanghai Instituteof Materia Medica Chinese Academy of Sciences Ben May Department for Cancer Research University of Chicago 

出 版 物：《Science China Chemistry》 (中国科学（化学英文版）)

年 卷 期：2014年第57卷第5期

页      面：732-738页

核心收录：

学科分类：081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070303[理学-有机化学] 0703[理学-化学] 

基　　金：supported by the National Science and Technology Major Project of the Ministry of Science and Technology of China(2012ZX09301001-007) the National Natural Science Foundation of China(31370814) the Shanghai Pujiang Program(13PJ1410300) the support of China Postdoctoral Science Foundation(2013M531236,2013M541567) 

主　　题：proteomics post-translational modification acetylation Staphylococcus aureus 

摘      要：The Gram-positive bacterium Staphylococcus aureus(***)is a wide spread common opportunistic pathogen that causes a wide variety of infectious diseases,from benign skin infections to life-threatening diseases such as the methicillin-resistant Staphylococcus aureus(MRSA)*** emerging evidence suggests that lysine acetylation may play critical roles in bacterial physiology,the atlas of acetylome in *** has not been *** comprehensively profile protein lysine acetylation in ***,we used an integrated approach that combined immune affinity peptide enrichment using anti-lysine acetylation antibody,high-pH HPLC fractionation,and HPLC/mass spectrometry *** study led to the identification of 1361 non-redundant acetylation sites on 412 proteins found in a search of *** protein database extracted from the Swiss-Prot *** further performed bioinformatic analysis to characterize this modification,including gene ontology annotation,protein-protein interaction,and domain analysis of the acetylation *** found that the acetylated proteins were enriched in multiple biological pathways,such as ribosomal function and energy *** data provides a rich source for functional studies of lysine acetylation in ***.