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J. Biol. Chem., Vol. 277, Issue 27, 24530-24537, July 5, 2002
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From the 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 hFBH1 (human F-box DNA
helicase 1). Recombinant hFBH1, containing
glutathione S-transferase at the N terminus, was expressed
in Sf9 cells and purified. In this report, we show that hFBH1
exhibited DNA-dependent ATPase and DNA unwinding activities that displace duplex DNA in the 3' to 5' direction. The hFBH1 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 hFBH1 as an F-box protein displayed ubiquitin ligase
activity. We demonstrate that hFBH1 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 are discussed with regard
to regulation of DNA metabolism.
National Creative Research Initiative Center
for Cell Cycle Control, Samsung Biomedical Research Institute,
Sungkyunkwan University School of Medicine, 300 Chunchun-Dong,
Changan-Ku, Suwon, Kyunggi-Do, 440-746, Korea, the
§ Department of Pharmacology, Dong-A University College of
Medicine, 3-ga, Tongdaesin-Dong, Seo-Gu, Busan, 602-103, Korea, and
the ¶ Derald H. Ruttenberg Cancer Center, The Mount Sinai School
of Medicine, New York, New York 10029-6574
To whom correspondence should be addressed. Tel.:
82-31-299-6440; Fax: 82-31-299-6435; E-mail:
ysseo@med.skku.ac.kr.
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