Unknown

Dataset Information

0

Identification of the structural and functional human homolog of the yeast ubiquitin conjugating enzyme UBC9.


ABSTRACT: Ubiquitin conjugating enzymes (UBCs) are a family of proteins directly involved in ubiquitination of proteins. Ubiquitination is known to be involved in control of a variety of cellular processes, including cell proliferation, through the targeting of key regulatory proteins for degradation. The ubc9 gene of the yeast Saccharomyces cerevisiae (Scubc9) is an essential gene which is required for cell cycle progression and is involved in the degradation of S phase and M phase cyclins. We have identified a human homolog of Scubc9 (termed hubc9) using the two hybrid screen for proteins that interact with the human papillomavirus type 16 E1 replication protein. The hubc9 encoded protein shares a very high degree of amino acid sequence similarity with ScUBC9 and with the homologous hus5+ gene product of Schizosaccharomyces pombe. Genetic complementation experiments in a S.cerevisiae ubc9ts mutant reveal that hUBC9 can substitute for the function of ScUBC9 required for cell cycle progression.

SUBMITTER: Yasugi T 

PROVIDER: S-EPMC145898 | biostudies-other | 1996 Jun

REPOSITORIES: biostudies-other

altmetric image

Publications

Identification of the structural and functional human homolog of the yeast ubiquitin conjugating enzyme UBC9.

Yasugi T T   Howley P M PM  

Nucleic acids research 19960601 11


Ubiquitin conjugating enzymes (UBCs) are a family of proteins directly involved in ubiquitination of proteins. Ubiquitination is known to be involved in control of a variety of cellular processes, including cell proliferation, through the targeting of key regulatory proteins for degradation. The ubc9 gene of the yeast Saccharomyces cerevisiae (Scubc9) is an essential gene which is required for cell cycle progression and is involved in the degradation of S phase and M phase cyclins. We have ident  ...[more]

Similar Datasets

| S-EPMC5430876 | biostudies-literature
| S-EPMC3056393 | biostudies-literature
| S-EPMC3840907 | biostudies-literature
| S-EPMC2822102 | biostudies-literature
| S-EPMC2222581 | biostudies-literature
| S-EPMC2765280 | biostudies-literature
| S-EPMC7613103 | biostudies-literature
| S-EPMC3030398 | biostudies-literature
| S-EPMC3412965 | biostudies-literature
| S-EPMC107327 | biostudies-literature