Abstract

The N-end rule relates the in vivo half-life of a protein to the identity of its amino-terminal residue. Distinct versions of the N-end rule operate in all organisms examined, from mammals to bacteria. We show that UBC2(RAD6), one of at least seven ubiquitin-conjugating enzymes in the yeast Saccharomyces cerevisiae, is essential for multiubiquitination and degradation of the N-end rule substrates. We also show that UBC2 is physically associated with UBR1, the recognition component of the N-end rule pathway. These results indicate that some of the UBC2 functions, which include DNA repair, induced mutagenesis, sporulation, and regulation of retrotransposition, are mediated by protein degradation via the N-end rule pathway.

Keywords

Saccharomyces cerevisiaeUbiquitin-conjugating enzymeUbiquitinsUbiquitinBiochemistryBiologyEnzymeMutagenesisDNAYeastGeneticsUbiquitin ligaseMutationGene

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Publication Info

Year
1991
Type
article
Volume
88
Issue
16
Pages
7351-7355
Citations
266
Access
Closed

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R. Jürgen Dohmen, Kiran Madura, Bonnie Bartel et al. (1991). The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating enzyme.. Proceedings of the National Academy of Sciences , 88 (16) , 7351-7355. https://doi.org/10.1073/pnas.88.16.7351

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DOI
10.1073/pnas.88.16.7351