Structural and functional insights into the activation of the dual incision activity of UvrC, a key player in bacterial NER.
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
11 04 2023
11 04 2023
Historique:
accepted:
06
02
2023
revised:
10
01
2023
received:
28
09
2022
medline:
12
4
2023
pubmed:
5
3
2023
entrez:
4
3
2023
Statut:
ppublish
Résumé
Bacterial nucleotide excision repair (NER), mediated by the UvrA, UvrB and UvrC proteins is a multistep, ATP-dependent process, that is responsible for the removal of a very wide range of chemically and structurally diverse DNA lesions. DNA damage removal is performed by UvrC, an enzyme possessing a dual endonuclease activity, capable of incising the DNA on either side of the damaged site to release a short single-stranded DNA fragment containing the lesion. Using biochemical and biophysical approaches, we have probed the oligomeric state, UvrB- and DNA-binding abilities and incision activities of wild-type and mutant constructs of UvrC from the radiation resistant bacterium, Deinococcus radiodurans. Moreover, by combining the power of new structure prediction algorithms and experimental crystallographic data, we have assembled the first model of a complete UvrC, revealing several unexpected structural motifs and in particular, a central inactive RNase H domain acting as a platform for the surrounding domains. In this configuration, UvrC is maintained in a 'closed' inactive state that needs to undergo a major rearrangement to adopt an 'open' active state capable of performing the dual incision reaction. Taken together, this study provides important insight into the mechanism of recruitment and activation of UvrC during NER.
Identifiants
pubmed: 36869664
pii: 7068374
doi: 10.1093/nar/gkad108
pmc: PMC10085695
doi:
Substances chimiques
Bacterial Proteins
0
DNA Helicases
EC 3.6.4.-
DNA, Bacterial
0
Endodeoxyribonucleases
EC 3.1.-
UvrC protein, E coli
EC 3.1.25.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2931-2949Informations de copyright
© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.
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