Snaith Hilary A, Marlett John, Forsburg Susan L
The Salk Institute, 10010 North Torrey Pines Road, La Jolla, CA 92037-1099, USA.
Curr Genet. 2003 Oct;44(1):38-48. doi: 10.1007/s00294-003-0424-1. Epub 2003 Jul 9.
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.
我们报告了在裂殖酵母粟酒裂殖酵母中鉴定出一种新型的Cdc25样蛋白磷酸酶Ibp1。Ibp1与Cdc25双特异性磷酸酶的催化亚基密切相关,并在体外具有磷酸酶活性。催化活性Ibp1的过量产生强烈抑制复制起始激酶Hsk1p(蛋白激酶Cdc7家族的成员)中的突变,并微弱抑制Rad4/Cut5(一种与DNA聚合酶ε相关的因子)的突变。Ibp1不是生存所必需的,这表明它可能是S期DNA复制或染色体结构的非必需调节因子。