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Papers In Press, published online ahead of print April 15, 2002
Molecular and Cellular Biology, Sungkyunkwan University School of Medicine, Suwon, Kyunggi 440-746
Corresponding Author: ysseo{at}med.skku.ac.kr
We have identified a novel DNA helicase in humans that belongs to members of the superfamily I helicase, and found that it contains a well-conserved F-box motif at its N-terminus. We have named the enzyme human F-box DNA Helicase (hFDH). Recombinant hFDH, containing glutathione-S transferase at the N-terminus, was expressed in Sf9 cells and purified. In this report, we show that hFDH exhibited DNA-dependent ATPase and DNA unwinding activities that displaces duplex DNA in the 3’ to 5’ direction. The hFDH enzyme interacted with human SKP1 and formed an SCF (SKP1/Cullin/F-box) complex together with human Cullin and ROC1. In addition, the SCF complex containing hFDH as a F-box protein displayed ubiquitin ligase activity. We demonstrate that hFDH is the first F-box protein that possesses intrinsic enzyme activity. The potential role of the F-box motif and the helicase activity of the enzyme is discussed with regard to regulation of DNA metabolism.
J. Biol. Chem, 10.1074/jbc.M201612200
Submitted on February 17, 2002
Revised on April 5, 2002
Accepted on April 14, 2002
The novel human DNA helicase hFDH is an F-box protein
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