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Junction resolving enzymes use multivalency to keep the Holliday junction dynamic

Holliday junction (HJ) resolution by its 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, i...

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Autores principales: Zhou, Ruobo, Yang, Olivia, Déclais, Anne-Cécile, Jin, Hyeonseok, Gwon, Gwang Hyeon, Freeman, Alasdair D. J., Cho, Yunje, Lilley, David M. J., Ha, Taekjip
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6377835/
https://www.ncbi.nlm.nih.gov/pubmed/30664685
http://dx.doi.org/10.1038/s41589-018-0209-y
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author Zhou, Ruobo
Yang, Olivia
Déclais, Anne-Cécile
Jin, Hyeonseok
Gwon, Gwang Hyeon
Freeman, Alasdair D. J.
Cho, Yunje
Lilley, David M. J.
Ha, Taekjip
author_facet Zhou, Ruobo
Yang, Olivia
Déclais, Anne-Cécile
Jin, Hyeonseok
Gwon, Gwang Hyeon
Freeman, Alasdair D. J.
Cho, Yunje
Lilley, David M. J.
Ha, Taekjip
author_sort Zhou, Ruobo
collection PubMed
description Holliday junction (HJ) resolution by its 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.
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spelling pubmed-63778352019-07-21 Junction resolving enzymes use multivalency to keep the Holliday junction dynamic Zhou, Ruobo Yang, Olivia Déclais, Anne-Cécile Jin, Hyeonseok Gwon, Gwang Hyeon Freeman, Alasdair D. J. Cho, Yunje Lilley, David M. J. Ha, Taekjip Nat Chem Biol Article Holliday junction (HJ) resolution by its 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. 2019-01-21 2019-03 /pmc/articles/PMC6377835/ /pubmed/30664685 http://dx.doi.org/10.1038/s41589-018-0209-y Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Zhou, Ruobo
Yang, Olivia
Déclais, Anne-Cécile
Jin, Hyeonseok
Gwon, Gwang Hyeon
Freeman, Alasdair D. J.
Cho, Yunje
Lilley, David M. J.
Ha, Taekjip
Junction resolving enzymes use multivalency to keep the Holliday junction dynamic
title Junction resolving enzymes use multivalency to keep the Holliday junction dynamic
title_full Junction resolving enzymes use multivalency to keep the Holliday junction dynamic
title_fullStr Junction resolving enzymes use multivalency to keep the Holliday junction dynamic
title_full_unstemmed Junction resolving enzymes use multivalency to keep the Holliday junction dynamic
title_short Junction resolving enzymes use multivalency to keep the Holliday junction dynamic
title_sort junction resolving enzymes use multivalency to keep the holliday junction dynamic
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6377835/
https://www.ncbi.nlm.nih.gov/pubmed/30664685
http://dx.doi.org/10.1038/s41589-018-0209-y
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