The novel human DNA helicase hFBH1 is an F-box protein

Cited 56 time in webofscience Cited 55 time in scopus
  • Hit : 400
  • Download : 0
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 ((S) under bar KP1/(C) under bar ullin/(F) under bar -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.
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Issue Date
2002-07
Language
English
Article Type
Article
Keywords

KINASE-ACTIVATING KINASE; CELL-CYCLE; SACCHAROMYCES-CEREVISIAE; PROTEOLYSIS; IDENTIFICATION; METABOLISM; SEQUENCE; ENGINE; MOTIF; SGS1

Citation

JOURNAL OF BIOLOGICAL CHEMISTRY, v.277, no.27, pp.24530 - 24537

ISSN
0021-9258
DOI
10.1074/jbc.M201612200
URI
http://hdl.handle.net/10203/82962
Appears in Collection
BS-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 56 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0