The short-lived MATα2 transcriptional regulator is ubiquitinated in vivo
Abstract
The substrates of ubiquitin-dependent proteolytic pathways include both damaged or otherwise abnormal proteins and undamaged proteins that are naturally short-lived. Few specific examples of the latter class have been identified, however. Previous work has shown that the cell type-specific MAT-alpha-2 repressor of the yeast Saccharomyces cerevisiae is an extremely short-lived protein. We now demonstrate that alpha-2 is conjugated to ubiquitin in vivo. More than one lysine residue of alpha-2 can be joined to ubiquitin, and some of the ubiquitin moieties form a Lys48-linked multiubiquitin chain. Overexpression of degradation-impaired ubiquitin variants was used to show that at least a significant fraction of alpha-2 degradation is dependent on its ubiquitination.
Additional Information
© 1991 by the National Academy of Sciences. Communicated by Paul Schimmel, February S, 1991 (received for review December 18, 1990). We thank Bonnie Bartel and Peter Kolodziej for the 12CA5 antibody, Bonnie Bartel and John Tobias for comments on the manuscript, and Barbara Doran for secretarial assistance. This work was supported by grants to A.V. from the National Institutes of Health (DK39520 and AG08991) and an American Cancer Society grant (IRG41-32-1) to M.H. 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 - HOCpnas91.pdf
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Additional details
- PMCID
- PMC51714
- Eprint ID
- 1570
- Resolver ID
- CaltechAUTHORS:HOCpnas91
- NIH
- DK39520
- NIH
- AG08991
- American Cancer Society
- IRG41-32-1
- Created
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2006-01-30Created from EPrint's datestamp field
- Updated
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2021-11-08Created from EPrint's last_modified field