Structural characterization of mouse HAUSP, a proteolysis regulator of p53
이혜진, 유경재, 백광현,
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이혜진 ( Lee Hye-Jin ) - Pochon CHA University CHA General Hospital Cell and Gene Therapy Research Institute
유경재 ( Yoo Kyong-Jai ) - Pochon CHA University CHA General Hospital Cell and Gene Therapy Research Institute
백광현 ( Baek Kwang-Hyun ) - Pochon CHA University CHA General Hospital Cell and Gene Therapy Research Institute
Abstract
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. mHAUSP cDNA consisted of 3,312 bp encodes 1,103 amino acids with a molecular weight of approximately 135 kDa containing highly conserved Cys, Asp (I), His, and Asn/Asp (II) domains. In this study, we carried out site?directed mutagenesis of 6 conserved amino acids (Cys224, Gln231, Asp296, His457, His465, and Asp482) in Cys box, QQD box, and His box. Interestingly, the conserved Gln 231 was not essential for the catalytic activity of mHAUSP. However, the other conserved amino acids were required for deubiquitinating activity of mHAUSP. We performed isopeptidase assay and confirmed that mHAUSP is able to remove ubiquitin from ubiquitinated substrates. In addition, we observed that mHAUSP induces apoptosis in HeLa cells.
키워드
Apoptosis; Deubiquitinating enzyme; HAUSP; p53; Ubiquitin
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