Abstract
ALTHOUGH mitotic cyclins are well-known substrates for ubiquitin-mediated proteolysis at the metaphase–anaphase transition1–4, their degradation is not essential for separation of sister chromatids5–8; several lines of evidence suggest that proteolysis of other protein(s) is required, however4,6,9–11. Here we report the anaphase-specific proteolysis of the Schizosaccharomyces pombe Cut2 protein, which is essential for sister-chromatid separation12,13. Cut2 is located in the nucleus, where it is concentrated along the short metaphase spindle. The rapid degradation of Cut2 at anaphase requires its amino-terminal region and the activity of Cut9 (ref. 14), a component of the 20S cyclosome/ anaphase-promoting complex (APC), which is necessary for cyclin destruction3,4,11. Expression of non-degradable Cut2 blocks sister-chromatid separation but not cell-cycle progression. This defect can be overcome by grafting the N terminus of cyclin B onto the truncated Cut2, demonstrating that the regulated proteolysis of Cut2 is essential for sister-chromatid separation.
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Funabiki, H., Yamano, H., Kumada, K. et al. Cut2 proteolysis required for sister-chromatid separation in fission yeast. Nature 381, 438–441 (1996). https://doi.org/10.1038/381438a0
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DOI: https://doi.org/10.1038/381438a0
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