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Werner syndrome protein interacts with human flap endonuclease 1 and stimulates its cleavage activity.

The EMBO journal | Oct 15, 2001

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.

Pubmed ID: 11598021 RIS Download

Mesh terms: Adenosine Triphosphatases | Catalysis | DNA | DNA Helicases | DNA-Binding Proteins | Endodeoxyribonucleases | Enzyme Activation | Exodeoxyribonucleases | Exonucleases | Flap Endonucleases | HeLa Cells | Humans | Macromolecular Substances | Peptide Fragments | Proliferating Cell Nuclear Antigen | Protein Structure, Tertiary | RecQ Helicases | Recombinant Fusion Proteins | Replication Protein A | Werner Syndrome | Werner Syndrome Helicase