Identification of the structural and functional human homolog of the yeast ubiquitin conjugating enzyme UBC9
Author(s) -
Toshiharu Yasugi,
Peter M. Howley
Publication year - 1996
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/24.11.2005
Subject(s) - biology , schizosaccharomyces pombe , ubiquitin conjugating enzyme , complementation , schizosaccharomyces , saccharomyces cerevisiae , ubiquitin , biochemistry , f box protein , gene product , gene , ubiquitin ligase , genetics , microbiology and biotechnology , mutant , gene expression
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.
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