Cloning and characterization of the major AP endonuclease from Staphylococcus aureus.
AP endonuclease
Abasic sites
Base excision repair
DNA damage
DNA repair
Endonuclease IV
Nucleotide incision repair
Oxidative damage
Staphylococcus aureus
Journal
DNA repair
ISSN: 1568-7856
Titre abrégé: DNA Repair (Amst)
Pays: Netherlands
ID NLM: 101139138
Informations de publication
Date de publication:
11 2022
11 2022
Historique:
received:
25
04
2022
revised:
19
07
2022
accepted:
20
08
2022
pubmed:
12
9
2022
medline:
14
10
2022
entrez:
11
9
2022
Statut:
ppublish
Résumé
Apurinic/apyrimidinic (AP) endonucleases are key enzymes involved in the repair of abasic sites and DNA strand breaks. Complete genome analysis of Staphylococcus aureus identified a single AP endonuclease, SaNfo, which is a member of the endonuclease IV family exemplified by Escherichia coli Nfo. At present, it remains unknown whether SaNfo possesses DNA repair activities similar to its counterparts from E. coli and other bacteria. Here, we report that the purified SaNfo protein contains efficient AP endonuclease and nucleotide incision repair (NIR) activities. Optimal reaction conditions for SaNfo-catalysed AP endonuclease activity are high ionic strength and Mn
Identifiants
pubmed: 36088709
pii: S1568-7864(22)00123-9
doi: 10.1016/j.dnarep.2022.103390
pii:
doi:
Substances chimiques
Nucleotides
0
DNA
9007-49-2
Hydrogen Peroxide
BBX060AN9V
Endonucleases
EC 3.1.-
Deoxyribonuclease IV (Phage T4-Induced)
EC 3.1.21.2
DNA-(Apurinic or Apyrimidinic Site) Lyase
EC 4.2.99.18
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
103390Informations de copyright
Copyright © 2022 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that there are no conflicts of interest.