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

被引：164

作者：

Edwards, RJ ^{[1
]}

Bentley, NJ ^{[1
]}

Carr, AM ^{[1
]}

机构：

[1] Univ Sussex, MRC, Cell Mutat Unit, Brighton BN1 9RR, E Sussex, England

来源：

NATURE CELL BIOLOGY | 1999年 / 1卷 / 07期

基金：

欧盟地平线“2020”;

关键词：

D O I：

10.1038/15623

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

引用

页码：393 / 398

页数：6

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