Work

The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo.

Year: 1991

Type: article

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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.88.11.4606

Authors: M Hochstrasser, M J Ellison, V Chau, A Varshavsky

Institution: University of Chicago

Language: English

Topic: Ubiquitin and proteasome pathways

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute on Aging, National Institute of Diabetes and Digestive and Kidney Diseases

Awards: G56093450, STRESS, REPAIR, AND AGING, G7355241332, G9000237494