Escherichia coli DNA repair helicase Lhr is also a uracil-DNA glycosylase.
DNA repair
DNA replication
glycosylase
helicase
uracil
Journal
Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028
Informations de publication
Date de publication:
08 2023
08 2023
Historique:
revised:
24
06
2023
received:
16
01
2023
accepted:
27
06
2023
medline:
21
8
2023
pubmed:
15
7
2023
entrez:
14
7
2023
Statut:
ppublish
Résumé
DNA glycosylases protect genetic fidelity during DNA replication by removing potentially mutagenic chemically damaged DNA bases. Bacterial Lhr proteins are well-characterized DNA repair helicases that are fused to additional 600-700 amino acids of unknown function, but with structural homology to SecB chaperones and AlkZ DNA glycosylases. Here, we identify that Escherichia coli Lhr is a uracil-DNA glycosylase (UDG) that depends on an active site aspartic acid residue. We show that the Lhr DNA helicase activity is functionally independent of the UDG activity, but that the helicase domains are required for fully active UDG activity. Consistent with UDG activity, deletion of lhr from the E. coli chromosome sensitized cells to oxidative stress that triggers cytosine deamination to uracil. The ability of Lhr to translocate single-stranded DNA and remove uracil bases suggests a surveillance role to seek and remove potentially mutagenic base changes during replication stress.
Substances chimiques
Uracil-DNA Glycosidase
EC 3.2.2.-
DNA
9007-49-2
Uracil
56HH86ZVCT
DNA Helicases
EC 3.6.4.-
Bacterial Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
298-306Subventions
Organisme : Biotechnology and Biological Sciences Research Council
Pays : United Kingdom
Informations de copyright
© 2023 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.
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