Structural and Functional Investigations of the N-Terminal Ubiquitin Binding Region of Usp25.

ABSTRACT: Ubiquitin-specific protease 25 (Usp25) is a deubiquitinase that is involved in multiple biological processes. The N-terminal ubiquitin-binding region (UBR) of Usp25 contains one ubiquitin-associated domain, one small ubiquitin-like modifier (SUMO)-interacting motif and two ubiquitin-interacting motifs. Previous studies suggest that the covalent sumoylation in the UBR of Usp25 impairs its enzymatic activity. Here, we raise the hypothesis that non-covalent binding of SUMO, a prerequisite for efficient sumoylation, will impair Usp25's catalytic activity as well. To test our hypothesis and elucidate the underlying molecular mechanism, we investigated the structure and function of the Usp25 N-terminal UBR. The solution structure of Usp25_1-146 is obtained, and the key residues respons

SUBMITTER: Yang Y 

PROVIDER: S-EPMC5444020 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature