Functional and physical interaction between WRN helicase and human replication protein A.

@article{Brosh1999FunctionalAP,
  title={Functional and physical interaction between WRN helicase and human replication protein A.},
  author={Robert M. Brosh and David K. Orren and Johan Nehlin and Pernille Ravn and Mark Kulie Kenny and Amrita Machwe and Vilhelm A. Bohr},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 26},
  pages={
          18341-50
        }
}
The human premature aging disorder Werner syndrome (WS) is associated with a large number of symptoms displayed in normal aging. The WRN gene product, a DNA helicase, has been previously shown to unwind short DNA duplexes (</=53 base pairs) in a reaction stimulated by single-stranded DNA-binding proteins. We have studied the helicase activity of purified WRN protein on a variety of DNA duplex substrates to characterize the unwinding properties of the enzyme in greater detail. WRN helicase can… CONTINUE READING

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