Junction resolving enzymes use multivalency to keep the Holliday junction dynamic.
Animals
Arabidopsis Proteins
Chromosome Segregation
/ genetics
DNA Repair
/ physiology
DNA, Cruciform
/ metabolism
DNA-Binding Proteins
/ physiology
Deoxyribonuclease I
Endodeoxyribonucleases
Endonucleases
Escherichia coli Proteins
Fluorescence Resonance Energy Transfer
/ methods
Holliday Junction Resolvases
/ metabolism
Humans
Protein Binding
Recombination, Genetic
/ genetics
Single Molecule Imaging
/ methods
Substrate Specificity
Journal
Nature chemical biology
ISSN: 1552-4469
Titre abrégé: Nat Chem Biol
Pays: United States
ID NLM: 101231976
Informations de publication
Date de publication:
03 2019
03 2019
Historique:
received:
15
10
2017
accepted:
30
11
2018
pubmed:
22
1
2019
medline:
20
4
2019
entrez:
22
1
2019
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 30664685
doi: 10.1038/s41589-018-0209-y
pii: 10.1038/s41589-018-0209-y
pmc: PMC6377835
mid: NIHMS1515515
doi:
Substances chimiques
Arabidopsis Proteins
0
DNA, Cruciform
0
DNA-Binding Proteins
0
Escherichia coli Proteins
0
ruvC protein, E coli
0
Endodeoxyribonucleases
EC 3.1.-
Endonucleases
EC 3.1.-
MUS81 protein, human
EC 3.1.-
Holliday Junction Resolvases
EC 3.1.21.-
XPG-like endonuclease 1, Arabidopsis
EC 3.1.21.-
Deoxyribonuclease I
EC 3.1.21.1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
269-275Subventions
Organisme : Cancer Research UK
ID : 11722
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : B17092
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/E001777/1
Pays : United Kingdom
Organisme : NIGMS NIH HHS
ID : R35 GM122569
Pays : United States
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