Junction resolving enzymes use multivalency to keep the Holliday junction dynamic

Ruobo Zhou (Lead / Corresponding author), Olivia Yang, Anne-Cecile Declais, Hyeonseok Jin, Gwang Hyeon Gwon, Alasdair Freeman, Yunje Cho, David Lilley, Taekjip Ha (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    20 Citations (Scopus)
    158 Downloads (Pure)

    Abstract

    Holliday junction (HJ) resolution by resolving enzymes is essential for chromosome segregation and recombination-mediated DNA repair. HJs undergo two types of structural dynamics that determine the outcome of recombination: conformer exchange between two isoforms and branch migration. However, it is unknown how the preferred branch point and conformer are achieved between enzyme binding and HJ resolution given the extensive binding interactions seen in static crystal structures. Single-molecule fluorescence resonance energy transfer analysis of resolving enzymes from bacteriophages (T7 endonuclease I), bacteria (RuvC), fungi (GEN1) and humans (hMus81-Eme1) showed that both types of HJ dynamics still occur after enzyme binding. These dimeric enzymes use their multivalent interactions to achieve this, going through a partially dissociated intermediate in which the HJ undergoes nearly unencumbered dynamics. This evolutionarily conserved property of HJ resolving enzymes provides previously unappreciated insight on how junction resolution, conformer exchange and branch migration may be coordinated.

    Original languageEnglish
    Pages (from-to)269-275
    Number of pages7
    JournalNature Chemical Biology
    Volume15
    Issue number3
    Early online date21 Jan 2019
    DOIs
    Publication statusPublished - 1 Mar 2019

    ASJC Scopus subject areas

    • Molecular Biology
    • Cell Biology

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