Lysine acetylation is widespread on proteins of diverse function and localization in the protozoan parasite Toxoplasma gondii.

ABSTRACT: While histone proteins are the founding members of lysine acetylation substrates, it is now clear that hundreds of other proteins can be acetylated in multiple compartments of the cell. Our knowledge of the scope of this modification throughout the kingdom of life is beginning to emerge, as proteome-wide lysine acetylation has been documented in prokaryotes, Arabidopsis thaliana, Drosophila melanogaster, and human cells. Using liquid chromatography-tandem mass spectrometry (LC-MS/MS) to identify parasite peptides enriched by immunopurification with acetyl-lysine antibody, we produced the first proteome-wide analysis of acetylation for a protozoan organism, the opportunistic apicomplexan parasite Toxoplasma gondii. The results show that lysine acetylation is abundant in the actively prolife

SUBMITTER: Jeffers V 

PROVIDER: S-EPMC3370464 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature