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 journalArticle

4 Citations (Scopus)
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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

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