期刊
BIOCHEMICAL JOURNAL
卷 400, 期 -, 页码 53-62出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20060774
关键词
base excision repair; DNA damage checkpoint; DNA glycosylase; fission yeast; Hus1; MutY glycosylase homologue (MYH)
资金
- NCI NIH HHS [CA/ES78391] Funding Source: Medline
- NIGMS NIH HHS [GM35132, R01 GM035132] Funding Source: Medline
The MYH (MutY glycosylase homologue) increases replication fidelity by removing adenines or 2-hydroxyadenine misincorporated opposite GO (7,8-dihydro-8-oxo-guanine). The 9-1-1 complex (Rad9, Rad1 and Hus1 heterotrimer complex) has been suggested as a DNA damage sensor. Here, we report that hMYH (human MYH) interacts with hHus1 (human Hus1) and hRad1 (human Rad1), but not with hRad9. In addition, interactions between MYH and the 9-1-1 complex, from both the fission yeast Schizosaccharomyces pombe and human cells, are partially interchangeable. The major Hus1-binding site is localized to residues 295-350 of hMYH and to residues 245-293 of SpMYH (S. pombe MYH). Val(315) of hMYH and Ile(261) of SpMYH play important roles for their interactions with Hus1. hHus1 protein and the 9-1-1 complex of S. pombe can enhance the glycosylase activity of SpMYH. Moreover, the interaction of hMYH-hHus1 is enhanced following ionizing radiation. A significant fraction of the hMYH nuclear foci co-localizes with hRad9 foci in H2O2-treated cells. These results reveal that the 9-1-1 complex plays a direct role in base excision repair.
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