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Fission yeast Dss1 associates with the proteasome and is required for efficient ubiquitin-dependent proteolysis

Harley, Margaret E.; Pires, Isabel M. S.; Hughes, David A.; Pires, Isabel M.S.; Jossé, Lyne; Harley, Margaret E.; Monteiro dos Santos Pires, Isabel; Hughes, David A.

Authors

Margaret E. Harley

Isabel M. S. Pires

David A. Hughes

Isabel M.S. Pires

Lyne Jossé

Margaret E. Harley

David A. Hughes



Abstract

Human DSS1 associates with BRCA2, a tumour suppressor protein required for efficient recombinational DNA repair, but the biochemical function of DSS1 is not known. Orthologues of DSS1 are found in organisms such as budding yeast and fission yeast that do not have BRCA2-related proteins, indicating that DSS1 has a physiological role independent of BRCA2. The DSS1 orthologue in Saccharomyces cerevisiae has been shown to associate with the 26 S proteasome and, in the present paper, we report that in the distantly related fission yeast Schizosaccharomyces pombe, Dss1 associates with the 19 S RP (regulatory particle) of the 26 S proteasome. A role for S. pombe Dss1 in proteasome function is supported by three lines of evidence. First, overexpression of two components of the 19 S RP, namely Pad1/Rpn11 and Mts3/Rpn12, rescued the temperature-sensitive growth defect of the dss1 mutant. Secondly, the dss1 mutant showed phenotypes indicative of a defect in proteasome function: growth of the dss1 mutant was inhibited by low concentrations of L-canavanine, an amino acid analogue, and cells of the dss1 mutant accumulated high molecular mass poly-ubiquitylated proteins. Thirdly, synthetic growth defects were found when the dss1 mutation was combined with mutations in other proteasome subunit genes. These findings show that DSS1 has an evolutionarily conserved role as a regulator of proteasome function and suggest that DSS1 may provide a link between BRCA2 and ubiquitin-mediated proteolysis in human cells.

Journal Article Type Article
Publication Date Jan 1, 2006
Journal The Biochemical journal
Print ISSN 1470-8728
Electronic ISSN 1470-8728
Publisher Portland Press
Peer Reviewed Peer Reviewed
Volume 393
Issue 1
Pages 303-309
APA6 Citation Jossé, L., Harley, M. E., Monteiro dos Santos Pires, I., & Hughes, D. A. (2006). Fission yeast Dss1 associates with the proteasome and is required for efficient ubiquitin-dependent proteolysis. Biochemical Journal, 393(1), 303-309. doi:10.1042/BJ20051238
DOI https://doi.org/10.1042/BJ20051238
Keywords Cell Biology; Biochemistry; Molecular Biology
Publisher URL http://www.biochemj.org/content/393/1/303
PMID 16149916
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