Biochemical and structural characterization of the Holliday junction resolvase RuvC from Pseudomonas aeruginosa.
Biochemical characterization
Crystal structure
Holliday junction
Pseudomonas aeruginosa
RuvC
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
30 04 2020
30 04 2020
Historique:
received:
03
02
2020
accepted:
09
02
2020
pubmed:
23
2
2020
medline:
11
11
2020
entrez:
23
2
2020
Statut:
ppublish
Résumé
The Holliday junction, a four-way DNA structure, is an important intermediate of homologous recombination. Proper Holliday junction resolution is critical to complete the recombination process. In most bacterial cells, the Holliday junction cleavage is mainly performed by a specific endonuclease RuvC. Here, we describe the biochemical properties and the crystal structure of RuvC from an opportunistic pathogen, Pseudomonas aeruginosa (PaRuvC). PaRuvC specifically binds to the Holliday junction DNA and preferentially cleaves it at the consensus 5'-TTC-3'. PaRuvC uses Mg
Identifiants
pubmed: 32085896
pii: S0006-291X(20)30330-2
doi: 10.1016/j.bbrc.2020.02.062
pii:
doi:
Substances chimiques
Bacterial Proteins
0
DNA, Cruciform
0
Holliday Junction Resolvases
EC 3.1.21.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
265-271Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare no conflict of interests.