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- W2066253067 abstract "Werner syndrome (WS) is a human premature aging disorder characterized by chromosomal instability. The cellular defects of WS presumably reflect compromised or aberrant function of a DNA metabolic pathway that under normal circumstances confers stability to the genome. We report a novel interaction of the WRN gene product with the human 5' flap endonuclease/5'-3' exonuclease (FEN-1), a DNA structure-specific nuclease implicated in DNA replication, recombination and repair. WS protein (WRN) dramatically stimulates the rate of FEN-1 cleavage of a 5' flap DNA substrate. The WRN-FEN-1 functional interaction is independent of WRN catalytic function and mediated by a 144 amino acid domain of WRN that shares homology with RecQ DNA helicases. A physical interaction between WRN and FEN-1 is demonstrated by their co-immunoprecipitation from HeLa cell lysate and affinity pull-down experiments using a recombinant C-terminal fragment of WRN. The underlying defect of WS is discussed in light of the evidence for the interaction between WRN and FEN-1." @default.
- W2066253067 created "2016-06-24" @default.
- W2066253067 creator A5036007045 @default.
- W2066253067 date "2001-10-15" @default.
- W2066253067 modified "2023-10-06" @default.
- W2066253067 title "Werner syndrome protein interacts with human flap endonuclease 1 and stimulates its cleavage activity" @default.
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- W2066253067 doi "https://doi.org/10.1093/emboj/20.20.5791" @default.
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