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pubmed-article:1647011pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:1647011pubmed:articleTitleThe short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo.lld:pubmed
pubmed-article:1647011pubmed:affiliationDepartment of Biochemistry and Molecular Biology, University of Chicago, IL 60637.lld:pubmed
pubmed-article:1647011pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1647011pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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