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Cdc34 Self-Association Is Facilitated by Ubiquitin Thiolester Formation and Is Required for Its Catalytic Activity

Using a coimmunoprecipitation strategy, we showed that the Cdc34 ubiquitin (Ub)-conjugating enzyme from Saccharomyces cerevisiae self-associates in cell lysates, thereby indicating an in vivo interaction. The ability of Cdc34 to interact with itself is not dependent on its association with the ubiqu...

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Библиографические подробности
Опубликовано в::Mol Cell Biol
Главные авторы: Varelas, Xaralabos, Ptak, Christopher, Ellison, Michael J.
Формат: Artigo
Язык:Inglês
Опубликовано: Taylor & Francis 2003
Предметы:
Online-ссылка:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC165730/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12861024/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/MCB.23.15.5388-5400.2003
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