Autocatalytic activity of the ubiquitin-specific protease domain of herpes simplex virus 1 VP1-2.

ABSTRACT: The herpes simplex virus (HSV) tegument protein VP1-2 is essential for virus entry and assembly. VP1-2 also contains a highly conserved ubiquitin-specific protease (USP) domain within its N-terminal region. Despite conservation of the USP and the demonstration that it can act on artificial substrates such as polyubiquitin chains, identification of the relevance of the USP in vivo to levels or function of any substrate remains limited. Here we show that HSV VP1-2 USP can act on itself and is important for stability. VP1-2 N-terminal variants encompassing the core USP domain itself were not affected by mutation of the catalytic cysteine residue (C65). However, extending the N-terminal region resulted in protein species requiring USP activity for accumulation. In this context, C65A mutation r

SUBMITTER: Bolstad M 

PROVIDER: S-EPMC3165783 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature