Cloning and characterization of human ubiquitin binding enzyme 2 cDNA.
- Author:
Guangtao LI
1
;
Hongyan LÜ
;
Yan ZHOU
;
Jian JIN
;
Keyi JIANG
;
Xiaozhong PENG
;
Jiangang YUAN
;
Boqin QIANG
Author Information
- Publication Type:Journal Article
- MeSH: Amino Acid Sequence; Animals; Base Sequence; Cloning, Molecular; DNA, Complementary; genetics; Female; Humans; Mice; Molecular Sequence Data; Myocardium; metabolism; Pancreas; metabolism; Placenta; metabolism; Rats; Sequence Alignment; Sequence Analysis, DNA; Ubiquitin; genetics; Ubiquitin-Conjugating Enzymes; biosynthesis; chemistry; genetics
- From: Chinese Medical Sciences Journal 2002;17(1):7-12
- CountryChina
- Language:English
-
Abstract:
OBJECTIVETo clone and identify the gene encoding human ubiquitin binding enzyme 2 and study its expression pattern.
METHODSAccording to the sequence of human EST, which is highly homologous to the mouse ubiquitin binding/conjugating enzyme (E2), primers were synthesized to screen the human fetal brain cDNA library. The gene was analyzed by bioinformatics technique and its expression pattern was studied by using multiple-tissue Northern blot.
RESULTSTwo cDNA clones encoding human ubiquitin conjugating enzyme have been isolated and identified. Both containing the ubiquitin conjugating domain, the 2 cDNA clones are 88% identical in amino acid sequences and splicing isoforms to each other only with an exon excised to form the short sequence. They belong to a highly conserved and widely expressed E2 enzyme family. Northern blot shows that they are expressed exclusively in adult human heart, placenta, and pancreas but no transcripts can be detected in brain, lung, liver, skeletal muscle or kidney.
CONCLUSIONSThe gene encoding human ubiquitin binding enzyme is expressed under temporal control. As a key enzyme in the degradation of proteins, ubiquitin conjugating enzymes play a central role in the expression regulation on the level of post-translation.