The novel human DNA helicase hFBH1 is an F-box protein.
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.
Mesh Terms:
Amino Acid Sequence, Animals, Cell Line, DNA Helicases, DNA Primers, DNA-Binding Proteins, Escherichia coli Proteins, Humans, Molecular Sequence Data, Protein Conformation, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Spodoptera, Transfection
Amino Acid Sequence, Animals, Cell Line, DNA Helicases, DNA Primers, DNA-Binding Proteins, Escherichia coli Proteins, Humans, Molecular Sequence Data, Protein Conformation, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Spodoptera, Transfection
J. Biol. Chem.
Date: Jul. 05, 2002
PubMed ID: 11956208
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