A novel ubiquitin carboxyl terminal hydrolase is involved in toad oocyte maturation.
p28, a 28kD protein from toad (Bufo bufo gargarizans) oocytes, was identified by using p13(suc1)-agarose affinity chromatography. Sequence homology analysis of the full-length cDNA of p28 (Gene Bank accession number: AF 314091) indicated that it encodes a protein containing 224 amino-acids with about 55% identities and more than 70% positives to human, rat or mouse UCH-L1, and contains homological functional domains of UCH family. Anti-p28 monoclonal antibody, on injecting into the oocytes, could inhibit the progesterone-induced resumption of meiotic division in a dose-dependent manner. The recombinant protein p28 showed similar SDS/PAGE behaviors to the native one, and promoted ubiquitin ethyl ester hydrolysis, a classical catalytic reaction for ubiquitin carboxyl terminal hydrolases (UCHs). The results in this paper reveal that a novel protein, p28, exists in the toad oocytes, is a UCH L1 homolog, was engaged in the process of progesterone-induced oocyte maturation possibly through an involvement in protein turnover and degradation.
Sun
Zhao Gui
ZG
National Laboratory of Contraceptives and Devices Research, Shanghai Institute of Planned Parenthood Research, China
Kong
Wei Hua
WH
Zhang
Yan Jun
YJ
Yan
Shan
S
Lu
Ji Ning
JN
Gu
Zheng
Z
Lin
Feng
F
Tso
Jia Ke
JK
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002023:Bufo bufo / Q000196:embryology*; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D005260:Female; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009865:Oocytes / Q000737:chemistry / Q000502:physiology*; D017386:Sequence Homology, Amino Acid; D014452:Ubiquitins / Q000737:chemistry*
D014452:Ubiquitins; D002265:Carboxylic Ester Hydrolases