Junction resolving enzymes use multivalency to keep the Holliday junction dynamic View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2019-03

AUTHORS

Ruobo Zhou, Olivia Yang, Anne-Cécile Déclais, Hyeonseok Jin, Gwang Hyeon Gwon, Alasdair D. J. Freeman, Yunje Cho, David M. J. Lilley, Taekjip Ha

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. More... »

PAGES

269-275

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41589-018-0209-y

DOI

http://dx.doi.org/10.1038/s41589-018-0209-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1111348288

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30664685


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Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

JSON-LD is a popular format for linked data which is fully compatible with JSON.

curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1038/s41589-018-0209-y'

N-Triples is a line-based linked data format ideal for batch operations.

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/s41589-018-0209-y'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/s41589-018-0209-y'

RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/s41589-018-0209-y'


 

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290 Department of Physics and Center for the Physics of Living Cells, University of Illinois at Urbana-Champaign, Champaign, IL, USA
291 Howard Hughes Medical Institute, Baltimore, MD, USA
292 rdf:type schema:Organization
293 https://www.grid.ac/institutes/grid.38142.3c schema:alternateName Harvard University
294 schema:name Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA
295 Department of Physics and Center for the Physics of Living Cells, University of Illinois at Urbana-Champaign, Champaign, IL, USA
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297 https://www.grid.ac/institutes/grid.49100.3c schema:alternateName Pohang University of Science and Technology
298 schema:name Department of Life Science, Pohang University of Science and Technology, Pohang, South Korea
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300 https://www.grid.ac/institutes/grid.8241.f schema:alternateName University of Dundee
301 schema:name Cancer Research UK Nucleic Acid Structure Research Group, School of Life Sciences, The University of Dundee, Dundee, UK
302 rdf:type schema:Organization
 




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