Cargando…
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...
Autores principales: | , , , , , , , , |
---|---|
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 |
_version_ | 1783395821446758400 |
---|---|
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. |
format | Online Article Text |
id | pubmed-6377835 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT zhouruobo junctionresolvingenzymesusemultivalencytokeepthehollidayjunctiondynamic AT yangolivia junctionresolvingenzymesusemultivalencytokeepthehollidayjunctiondynamic AT declaisannececile junctionresolvingenzymesusemultivalencytokeepthehollidayjunctiondynamic AT jinhyeonseok junctionresolvingenzymesusemultivalencytokeepthehollidayjunctiondynamic AT gwongwanghyeon junctionresolvingenzymesusemultivalencytokeepthehollidayjunctiondynamic AT freemanalasdairdj junctionresolvingenzymesusemultivalencytokeepthehollidayjunctiondynamic AT choyunje junctionresolvingenzymesusemultivalencytokeepthehollidayjunctiondynamic AT lilleydavidmj junctionresolvingenzymesusemultivalencytokeepthehollidayjunctiondynamic AT hataekjip junctionresolvingenzymesusemultivalencytokeepthehollidayjunctiondynamic |