Junction resolving enzymes use multivalency to keep the Holliday junction dynamic
SCIE
SCOPUS
- 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
- 2019-03
- 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
- https://oasis.postech.ac.kr/handle/2014.oak/95272
- DOI
- 10.1038/s41589-018-0209-y
- ISSN
- 1552-4450
- Article Type
- Article
- Citation
- Nature Chemical Biology, vol. 15, no. 3, page. 269 - +, 2019-03
- Files in This Item:
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.