New lysine-acetylated proteins screened by immunoaffinity and liquid chromatography-mass spectrometry  

作　　者：ZHANG Bing ZHAO Chao LUO KaiXuan YAN GuoQuan YAO Jun WANG YingYin LU HaoJie FAN HuiZhi YANG PengYuan 

机构地区：[1]Department of Chemistry,Fudan University,Shanghai 200433,China [2]Institutes of Biomedical Sciences,Fudan University,Shanghai 200032,China

出　　处：《Science China Chemistry》2010年第1期238-244,共7页中国科学（化学英文版）

基　　金：support from the National Natural Science Foundation of China(Grant Nos.20675020&20735005);the National Science Foundation for Post-doctor of China(Grant No.20080440075);the Shanghai Leading Academic Discipline Project(Grant No.B109);the Shanghai Municipal Health Bureau(Grant No.2008Y024);the Shanghai Postdoctoral Sustentation Fund

摘　　要：The lack of selective extraction specific for lysine-acetylated proteins has been a major problem in the field of acetylation biology,though acetylation plays a key role in many biological processes.In this paper,we report for the first time the proteomic screening of lysine-acetylated proteins from a mouse liver tissue,by a new approach of immunoaffinity purification of lysine-acetylated peptides combined with nano-HPLC/MS/MS analysis.We have found 20 lysine-acetylated proteins with 21 lysine-acetylated sites,among which 12 lysine-acetylated proteins and 16 lysine-acetylated sites have never been reported before.Notably,three acetyltransferases harboring in mitochondrion are newly discovered acetyltransferases responsible for the acetylation of nonhistone proteins.We have explored the significant patterns of residue preference by the hierarchical clustering analysis of amino acid residues surrounding acetylation sites,which could be helpful to the prediction of new sites of lysine acetylation.Our findings provide more candidates for studying the important roles played by acetylation in diverse cellular pathways and related human diseases.The lack of selective extraction specific for lysine-acetylated proteins has been a major problem in the field of acetylation biology,though acetylation plays a key role in many biological processes.In this paper,we report for the first time the proteomic screening of lysine-acetylated proteins from a mouse liver tissue,by a new approach of immunoaffinity purification of lysine-acetylated peptides combined with nano-HPLC/MS/MS analysis.We have found 20 lysine-acetylated proteins with 21 lysine-acetylated sites,among which 12 lysine-acetylated proteins and 16 lysine-acetylated sites have never been reported before.Notably,three acetyltransferases harboring in mitochondrion are newly discovered acetyltransferases responsible for the acetylation of nonhistone proteins.We have explored the significant patterns of residue preference by the hierarchical clustering analysis of amino acid residues surrounding acetylation sites,which could be helpful to the prediction of new sites of lysine acetylation.Our findings provide more candidates for studying the important roles played by acetylation in diverse cellular pathways and related human diseases.

关 键 词：lysine acetylation immunoaffinity purification liquid chromatography mass spectrometry 

分 类 号：O6[理学—化学]