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Ibp1p, a novel Cdc25-related phosphatase, suppresses Schizosaccharomyces pombe hsk1 (cdc7)

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Abstract.

We report the identification of a novel Cdc25-like protein phosphatase, Ibp1, in the fission yeast Schizosaccharomyces pombe. Ibp1 is closely related to the catalytic subunit of the Cdc25 dual-specificity phosphatases and has phosphatase activity in vitro. Over-production of catalytically active Ibp1 robustly suppresses a mutation in the replication initiation kinase Hsk1p, a member of the Cdc7 family of protein kinases and weakly suppresses mutation of Rad4/Cut5, a DNA polymerase ε-associated factor. Ibp1 is not required for viability, suggesting it may be a non-essential regulator of DNA replication or chromosome structure during S phase.

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Acknowledgements.

We thank Grant Brown and Julie Bailis for strains, Julie Bailis for preparation of the Mcm2 substrate, Julie Bailis, Mike Catlett, Eliana Gómez, Jeff Hodson, and Rania Siam for critical reading of the manuscript, and all members of the laboratory for helpful advice. H.A.S. was partly supported by the Ralph M Parsons Foundation. This work supported by American Cancer Society grant RPG-00-132-01-CCG to S.L.F.

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Correspondence to Susan L. Forsburg.

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Snaith, H.A., Marlett, J. & Forsburg, S.L. Ibp1p, a novel Cdc25-related phosphatase, suppresses Schizosaccharomyces pombe hsk1 (cdc7). Curr Genet 44, 38–48 (2003). https://doi.org/10.1007/s00294-003-0424-1

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