RRC ID 35395
著者 Zhang Z, Tan M, Xie Z, Dai L, Chen Y, Zhao Y.
タイトル Identification of lysine succinylation as a new post-translational modification.
ジャーナル Nat Chem Biol
Abstract Of the 20 ribosomally coded amino acid residues, lysine is the most frequently post-translationally modified, which has important functional and regulatory consequences. Here we report the identification and verification of a previously unreported form of protein post-translational modification (PTM): lysine succinylation. The succinyllysine residue was initially identified by mass spectrometry and protein sequence alignment. The identified succinyllysine peptides derived from in vivo proteins were verified by western blot analysis, in vivo labeling with isotopic succinate, MS/MS and HPLC coelution of their synthetic counterparts. We further show that lysine succinylation is evolutionarily conserved and that this PTM responds to different physiological conditions. Our study also implies that succinyl-CoA might be a cofactor for lysine succinylation. Given the apparent high abundance of lysine succinylation and the significant structural changes induced by this PTM, it is expected that lysine succinylation has important cellular functions.
巻・号 7(1)
ページ 58-63
公開日 2011-1-1
DOI 10.1038/nchembio.495
PII nchembio.495
PMID 21151122
PMC PMC3065206
MeSH Acyl Coenzyme A / metabolism Amino Acid Sequence Blotting, Western Chromatography, High Pressure Liquid Escherichia coli Proteins / chemistry Escherichia coli Proteins / metabolism Lysine / chemistry Lysine / metabolism* Mass Spectrometry Molecular Sequence Data Peptides / chemistry Peptides / metabolism Protein Processing, Post-Translational* Sequence Alignment Succinic Acid / chemistry Succinic Acid / metabolism*
IF 12.587
引用数 365
WOS 分野 BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
原核生物(大腸菌) ASKA library