Proteolytic elimination of N-myristoyl modifications by the Shigella virulence factor IpaJ.

ABSTRACT: Protein N-myristoylation is a 14-carbon fatty-acid modification that is conserved across eukaryotic species and occurs on nearly 1% of the cellular proteome. The ability of the myristoyl group to facilitate dynamic protein-protein and protein-membrane interactions (known as the myristoyl switch) makes it an essential feature of many signal transduction systems. Thus pathogenic strategies that facilitate protein demyristoylation would markedly alter the signalling landscape of infected host cells. Here we describe an irreversible mechanism of protein demyristoylation catalysed by invasion plasmid antigen J (IpaJ), a previously uncharacterized Shigella flexneri type III effector protein with cysteine protease activity. A yeast genetic screen for IpaJ substrates identified ADP-ribosylation fa

SUBMITTER: Burnaevskiy N 

PROVIDER: S-EPMC3722872 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature