A novel ubiquitin carboxyl terminal hydrolase is involved in toad oocyte maturation

• 来源期刊: 细胞研究(英文版)
• 学科: 生物学
• 关键词: p28, cDNA clone, recombinant expression, ubiquitin carboxyl terminal hydrolase, oocyte maturation.
• 年，卷（期）: 2002,（4）
• 页码范围: 199-206
• 页数: 8页
• 分类号: Q2
• 语种: 中文

摘要

p28, a 28kD protein from toad (Bufo bufo gargarizans) oocytes, was identified by using p13suc1-agaroseaffinity chromatography. Sequence homology analysis of the full-length cDNA of p28 (Gene Bank accessionnumber: AF 314091) indicated that it encodes a protein containing 224 amino-acids with about 55%iden-tities and more than 70%positives to human, rat or mouse UCH-L1, and contains homological functionaldomains of UCH family. Anti-p28 monoclonal antibody, on injecting into the oocytes, could inhibit theprogesterone-induced resumption of meiotic division in a dose-dependent manner. The recombinant proteinp28 showed similar SDS/PAGE behaviors to the native one, and promoted ubiquitin ethyl ester hydrolysis,a classical catalytic reaction for ubiquitin carboxyl terminai hydrolases (UCHs). The results in this paperreveal that a novel protein, p28, exists in the toad oocytes, is a UCH L1 homolog, was engaged in theprocess of progesterone-induced oocyte maturation possibly through an involvement in protein turnover anddegradation.