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 |