Journal
NUCLEIC ACIDS RESEARCH
Volume 35, Issue 8, Pages 2463-2472Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkm075
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Funding
- NCI NIH HHS [CA102271, R01 CA102271, R56 CA078391, R01 CA081063, CA78391, CA81063, R01 CA078391] Funding Source: Medline
- NIEHS NIH HHS [P01ES06676, P30 ES006676] Funding Source: Medline
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The checkpoint protein Rad9/Rad1/Hus1 heterotrimer (the 9-1-1 complex) is structurally similar to the proliferating cell nuclear antigen sliding clamp and has been proposed to sense DNA damage that leads to cell cycle arrest or apoptosis. Human (h) NEIL1 DNA glycosylase, an ortholog of bacterial Nei/Fpg, is involved in repairing oxidatively damaged DNA bases. In this study, we show that hNEIL1 interacts with hRad9, hRad1 and hHus1 as individual proteins and as a complex. Residues 290 350 of hNEIL1 are important for the 9-1-1 association. A significant fraction of the hNEIL1 nuclear foci co-localize with hRad9 foci in hydrogen peroxide treated cells. Human NEIL1 DNA glycosylase activity is significantly stimulated by hHus1, hRad1, hRad9 separately and the 9-1-1 complex. Thus, the 9-1-1 complex at the lesion sites serves as both a damage sensor to activate checkpoint control and a component of base excision repair.
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