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• W2123279486 abstract "ABSTRACT 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 ubiquitin ligase Skp1-Cdc53/Cul1-Hrt1-F-box complex. Rather, this interaction depends upon the integrity of the Cdc34∼Ub thiolester. Furthermore, several principal determinants within the Cdc34 catalytic domain, including the active-site cysteine, amino acid residues S73 and S97, and its catalytic domain insertion, also play a role in self-association. Mutational studies have shown that these determinants are functionally important in vivo and operate at the levels of both Cdc34∼Ub thiolester formation and Cdc34-mediated multi-Ub chain assembly. These determinants are spatially situated in a region that is close to the active site, corresponding closely to the previously identified E2-Ub interface. These observations indicate that the formation of the Cdc34∼Ub thiolester is important for Cdc34 self-association and that the interaction of Cdc34∼Ub thiolesters is in turn a prerequisite for both multi-Ub chain assembly and Cdc34's essential function(s). A conclusion from these findings is that the placement of ubiquitin on the Cdc34 surface is a structurally important feature of Cdc34's function." @default.
• W2123279486 created "2016-06-24" @default.
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• W2123279486 date "2003-08-01" @default.
• W2123279486 modified "2023-10-12" @default.
• W2123279486 title "Cdc34 Self-Association Is Facilitated by Ubiquitin Thiolester Formation and Is Required for Its Catalytic Activity" @default.
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• W2123279486 doi "https://doi.org/10.1128/mcb.23.15.5388-5400.2003" @default.
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