Ibp1p, a novel Cdc25-related phosphatase, suppresses Schizosaccharomyces pombe hsk1 ( cdc7).
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.
D000595:Amino Acid Sequence; D018797:Cell Cycle Proteins / Q000378:metabolism*; D004261:DNA Replication; D015966:Gene Expression Regulation, Fungal; D008969:Molecular Sequence Data; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D012568:Schizosaccharomyces / Q000235:genetics / Q000378:metabolism*; D029702:Schizosaccharomyces pombe Proteins / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D020687:cdc25 Phosphatases / Q000378:metabolism*
D018797:Cell Cycle Proteins; D029702:Schizosaccharomyces pombe Proteins; C094761:HSK1 protein, S pombe; D017346:Protein Serine-Threonine Kinases; D020687:cdc25 Phosphatases