Rad3-Rad26复合物独立于其他检查点蛋白对DNA损伤作出反应。

A Rad3-Rad26 complex responds to DNA damage independently of other checkpoint proteins.

作者信息

Edwards R J, Bentley N J, Carr A M

机构信息

MRC Cell Mutation Unit, Sussex University, Falmer BN1 9RR, UK.

出版信息

Nat Cell Biol. 1999 Nov;1(7):393-8. doi: 10.1038/15623.

DOI:10.1038/15623

PMID:10559981

Abstract

The conserved PIK-related kinase Rad3 is required for all DNA-integrity-checkpoint responses in fission yeast. Here we report a stable association between Rad3 and Rad26 in soluble protein extracts. Rad26 shows Rad3-dependent phosphorylation after DNA damage. Unlike phosphorylation of Hus1, Crb2/Rhp9, Cds1 and Chk1, phosphorylation of Rad26 does not require other known checkpoint proteins. Rad26 phosphorylation is the first biochemical marker of Rad3 function, indicating that Rad3-related checkpoint kinases may have a direct role in DNA-damage recognition.

摘要

保守的PIK相关激酶Rad3是裂殖酵母中所有DNA完整性检查点反应所必需的。在此，我们报道了在可溶性蛋白提取物中Rad3与Rad26之间存在稳定的关联。DNA损伤后，Rad26显示出依赖于Rad3的磷酸化。与Hus1、Crb2/Rhp9、Cds1和Chk1的磷酸化不同，Rad26的磷酸化不需要其他已知的检查点蛋白。Rad26磷酸化是Rad3功能的首个生化标志物，表明Rad3相关的检查点激酶可能在DNA损伤识别中具有直接作用。