Ontology highlight
ABSTRACT:
SUBMITTER: Chen Y
PROVIDER: S-EPMC2911958 | biostudies-literature | 2007 May
REPOSITORIES: biostudies-literature
Chen Yue Y Sprung Robert R Tang Yi Y Ball Haydn H Sangras Bhavani B Kim Sung Chan SC Falck John R JR Peng Junmin J Gu Wei W Zhao Yingming Y
Molecular & cellular proteomics : MCP 20070130 5
The positively charged lysine residue plays an important role in protein folding and functions. Neutralization of the charge often has a profound impact on the substrate proteins. Accordingly all the known post-translational modifications at lysine have pivotal roles in cell physiology and pathology. Here we report the discovery of two novel, in vivo lysine modifications in histones, lysine propionylation and butyrylation. We confirmed, by in vitro labeling and peptide mapping by mass spectromet ...[more]