AI Article Synopsis
- The mitotic separase (ESP1) is essential for cleaving Scc1 in cohesin, which allows sister chromatids to separate during anaphase and is also involved in DNA damage repair.
- Researchers identified 10 temperature-sensitive mutants of ESP1 in budding yeast, all of which had trouble separating sister chromatids at higher temperatures and showed varying sensitivities to drugs like benomyl and bleomycin.
- The study found that overexpressing securin helped some mutants but worsened conditions for others; additionally, a Drosophila protein, MPT5, was discovered to help suppress defects in these mutants, leading to further discussion on the roles of separase.
Article Abstract
The mitotic separase cleaves Scc1 in cohesin to allow sister chromatids to separate from each other upon anaphase onset. Separase is also required for DNA damage repair. Here, we isolated and characterized 10 temperature-sensitive (ts) mutants of separase ESP1 in the budding yeast Saccharomyces cerevisiae. All mutants were defective in sister chromatid separation at the restricted temperature. Some esp1-ts mutants were hypersensitive to the microtubule poison benomyl and/or the DNA-damaging agent bleomycin. Overexpression of securin alleviated the growth defect in some esp1-ts mutants, whereas it rather exacerbated it in others. The Drosophila Pumilio homolog MPT5 was isolated as a high-dosage suppressor of esp1-ts cells. We discuss various features of separase based on these findings.
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| http://dx.doi.org/10.1080/09168451.2015.1101337 | DOI Listing |
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