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Junction resolving enzymes use multivalency to keep the Holliday junction dynamic

Title
Junction resolving enzymes use multivalency to keep the Holliday junction dynamic
Authors
Zhou, R.Yang, O.Déclais, A.-C.Jin, H.Gwon, G.H.Freeman, A.D.J.Cho, Y.Lilley, D.M.J.Ha, T.
Date Issued
Mar-2019
Publisher
NATURE PUBLISHING GROUP
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.
URI
http://oasis.postech.ac.kr/handle/2014.oak/95272
ISSN
1552-4450
Article Type
Article
Citation
NATURE CHEMICAL BIOLOGY, vol. 15, no. 3, page. 269 - +, 2019-03
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 CHO, YUNJE
Dept of Life Sciences
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