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The structural and functional characterization of human RecQ4 reveals insights into its helicase mechanism

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  • Sebastian Kaiser

    (Rudolf-Virchow-Center for Experimental Biomedicine, Institute of Structural Biology)

  • Florian Sauer

    (Rudolf-Virchow-Center for Experimental Biomedicine, Institute of Structural Biology)

  • Caroline Kisker

    (Rudolf-Virchow-Center for Experimental Biomedicine, Institute of Structural Biology)

Abstract

RecQ4 is a member of the RecQ helicase family, an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair and replication. While reduced RecQ4 activity is associated with cancer predisposition and premature aging, RecQ4 upregulation is related to carcinogenesis and metastasis. Within the RecQ family, RecQ4 assumes an exceptional position, lacking several characteristic RecQ domains. Here we present the crystal structure of human RecQ4, encompassing the conserved ATPase core and a novel C-terminal domain that lacks resemblance to the RQC domain observed in other RecQ helicases. The new domain features a zinc-binding site and two distinct types of winged-helix domains, which are not involved in canonical DNA binding or helicase activity. Based on our structural and functional analysis, we propose that RecQ4 exerts a helicase mechanism, which may be more closely related to bacterial RecQ helicases than to its human family members.

Suggested Citation

  • Sebastian Kaiser & Florian Sauer & Caroline Kisker, 2017. "The structural and functional characterization of human RecQ4 reveals insights into its helicase mechanism," Nature Communications, Nature, vol. 8(1), pages 1-12, August.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15907
    DOI: 10.1038/ncomms15907
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    Cited by:

    1. Xiaohua Xu & Chou-Wei Chang & Min Li & Kenneth Omabe & Nhung Le & Yi-Hsuan Chen & Feng Liang & Yilun Liu, 2023. "DNA replication initiation factor RECQ4 possesses a role in antagonizing DNA replication initiation," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Anna C. Papageorgiou & Michaela Pospisilova & Jakub Cibulka & Raghib Ashraf & Christopher A. Waudby & Pavel Kadeřávek & Volha Maroz & Karel Kubicek & Zbynek Prokop & Lumir Krejci & Konstantinos Tripsi, 2023. "Recognition and coacervation of G-quadruplexes by a multifunctional disordered region in RECQ4 helicase," Nature Communications, Nature, vol. 14(1), pages 1-19, December.

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