The N-End Rule is Mediated by the UBC2(RAD6) Ubiquitin-Conjugating Enzyme
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.
Additional Information
© 1991 by National Academy of Sciences Communicated by Howard Green, May 22, 1991 We thank Daniel Gietz for the plasmids YEplacll2 and YEplacl95 and Barbara Doran for secretarial assistance. This research was supported by grants to A.V. from the National Institutes of Health (DK39520 and GM31530). R.J.D. and K.M. were supported by fellowships from the European Molecular Biology Organization and the American Cancer Society, respectively. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.Attached Files
Published - DOHpnas91.pdf
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Additional details
- PMCID
- PMC52293
- Eprint ID
- 729
- Resolver ID
- CaltechAUTHORS:DOHpnas91
- DK39520
- NIH
- GM31530
- NIH
- European Molecular Biology Organization (EMBO)
- American Cancer Society
- Created
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2005-09-21Created from EPrint's datestamp field
- Updated
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2021-11-08Created from EPrint's last_modified field