Format

Send to

Choose Destination
See comment in PubMed Commons below
Mol Cell Proteomics. 2009 Jan;8(1):45-52. doi: 10.1074/mcp.M800224-MCP200. Epub 2008 Aug 26.

Molecular characterization of propionyllysines in non-histone proteins.

Author information

1
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.

Abstract

Lysine propionylation and butyrylation are protein modifications that were recently identified in histones. The molecular components involved in the two protein modification pathways are unknown, hindering further functional studies. Here we report identification of the first three in vivo non-histone protein substrates of lysine propionylation in eukaryotic cells: p53, p300, and CREB-binding protein. We used mass spectrometry to map lysine propionylation sites within these three proteins. We also identified the first two in vivo eukaryotic lysine propionyltransferases, p300 and CREB-binding protein, and the first eukaryotic depropionylase, Sirt1. p300 was able to perform autopropionylation on lysine residues in cells. Our results suggest that lysine propionylation, like lysine acetylation, is a dynamic and regulatory post-translational modification. Based on these observations, it appears that some enzymes are common to the lysine propionylation and lysine acetylation regulatory pathways. Our studies therefore identified first several important players in lysine propionylation pathway.

PMID:
18753126
PMCID:
PMC2621001
DOI:
10.1074/mcp.M800224-MCP200
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Support Center