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• W2027179660 endingPage "4299" @default.
• W2027179660 startingPage "4294" @default.
• W2027179660 abstract "Ubiquitin-dependent proteolysis of the mitotic cyclins A and B is required for the completion of mitosis and entry into the next cell cycle. This process is catalyzed by the cyclosome, an approximately 22S particle that contains a cyclin-selective ubiquitin ligase activity, E3-C, that requires a cyclin-selective ubiquitin carrier protein (UBC) E2-C. Here we report the purification and cloning of E2-C from clam oocytes. The deduced amino acid sequence of E2-C indicates that it is a new UBC family member. Bacterially expressed recombinant E2-C is active in in vitro cyclin ubiquitination assays, where it exhibits the same substrate specificities seen with native E2-C. These results demonstrate that E2-C is not a homolog of UBC4 or UBC9, proteins previously suggested to be involved in cyclin ubiquitination, but is a new UBC family member with unique properties." @default.
• W2027179660 created "2016-06-24" @default.
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• W2027179660 date "1996-04-30" @default.
• W2027179660 modified "2023-10-02" @default.
• W2027179660 title "E2-C, a cyclin-selective ubiquitin carrier protein required for the destruction of mitotic cyclins." @default.
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• W2027179660 doi "https://doi.org/10.1073/pnas.93.9.4294" @default.
• W2027179660 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/39529" @default.
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