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

Jaehoon Kim, Jeong Hoon Kim, Sung Hak Lee, Do Hyung Kim, Ho Young Kang, Sung Ho Bae, Zhen Qiang Pan, Yeon Soo Seo

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)24530-24537
Number of pages8
JournalJournal of Biological Chemistry
Volume277
Issue number27
DOIs
StatePublished - 5 Jul 2002
Externally publishedYes

Fingerprint

Dive into the research topics of 'The novel human DNA helicase hFBH1 is an F-box protein'. Together they form a unique fingerprint.

Cite this