Defective mitosis due to a mutation in the gene for a fission yeast 26S protease subunit

WE have isolated a mutant, mts2 , in the fission yeast Schizosaccharomyces pombe which is defective in chromosome segregation. The predicted amino-acid sequence of the cloned mts2 + gene product is 75% identical to the S4 subunit of the human 26S ATP/ubiquitin-dependent protease 1 . The human S4 sub...

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Bibliographic Details
Published in:Nature (London) 1993-11, Vol.366 (6453), p.355-357
Main Authors: Gordon, Colin, McGurk, Gordon, Dillon, Patrick, Rosen, Craig, Hastie, Nicholas D
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biodegradation
Biological and medical sciences
Endopeptidases - genetics
Endopeptidases - physiology
Fundamental and applied biological sciences. Psychology
Genes, Fungal - physiology
Genetic Complementation Test
Genetics
Growth, nutrition, metabolism, transports, enzymes. Molecular biology
HeLa Cells
Humanities and Social Sciences
Humans
letter
Microbiology
Mitosis - drug effects
Mitosis - genetics
Molecular Sequence Data
multidisciplinary
Mutants
Mutation
Mycology
Schizosaccharomyces - cytology
Schizosaccharomyces - enzymology
Schizosaccharomyces - genetics
Schizosaccharomyces pombe
Schizosaccharomyces pombe Proteins
Science
Science (multidisciplinary)
Sequence Homology, Amino Acid
Temperature
Yeast
Yeasts
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Summary:WE have isolated a mutant, mts2 , in the fission yeast Schizosaccharomyces pombe which is defective in chromosome segregation. The predicted amino-acid sequence of the cloned mts2 + gene product is 75% identical to the S4 subunit of the human 26S ATP/ubiquitin-dependent protease 1 . The human S4 subunit complementary DNA expressed from an S. pombe expression plasmid can rescue an S. pombe mts2 gene disruption. Both observations demonstrate that the mts2 + gene is the S. pombe homologue of the human S4 subunit. In addition, we provide genetic evidence for a physical interaction between the S4 and the related S7 subunit in the 26S multiprotein protease. We show that polyubiquitin-conjugated proteins accumulate in the mts2 mutant at the restrictive temperature, demonstrating that the mutant has an in vivo defect in the ubiquitin-dependent proteolysis pathway. Finally, the phenotype for the mts2 mutant indicates that protein degradation by the 26S protease is essential not for entry into but for the completion of mitosis.
ISSN:0028-0836
1476-4687
DOI:10.1038/366355a0