| Literature DB >> 14508607 |
Hilary A Snaith1, John Marlett, Susan L Forsburg.
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 epsilon-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.Entities:
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Year: 2003 PMID: 14508607 DOI: 10.1007/s00294-003-0424-1
Source DB: PubMed Journal: Curr Genet ISSN: 0172-8083 Impact factor: 3.886