Molecular cloning of rHAUSP encoding a deubiquitinating enzyme in rat testis

The tumor suppressor protein p53 is stabilized by the herpes-virus-associated ubiquitin-specific protease (HAUSP), a deubiquitinating enzyme. We previously isolated and characterized a mouse orthologue of HAUSP, mHAUSP. In this study, we have identified a rat orthologue of HAUSP, rHAUSP, from the rat testis by RT-PCR using primers used for cloning mHAUSP. rHAUSP cDNA encodes 3,312 bp and 1,103 amino acids with a molecular weight of approximately 135 kDa containing highly conserved Cys, Asp (I), His, and Asn/Asp (II) domains characteristic of the ubiquitin-specific processing proteases. pi value of rHAUSP is 5.31. In vivo and in vitro deubiquitinating enzyme assays demonstrated that rHAUSP has deubiquitinating enzymatic activity. The over( expression of rHAUSP induced cell death of cervical adeno-carcinoma cells.