Contribution of GO System Glycosylases to Mutation Prevention in Caulobacter crescentus.


Journal

Environmental and molecular mutagenesis
ISSN: 1098-2280
Titre abrégé: Environ Mol Mutagen
Pays: United States
ID NLM: 8800109

Informations de publication

Date de publication:
02 2020
Historique:
received: 23 04 2019
revised: 29 08 2019
accepted: 12 09 2019
pubmed: 1 10 2019
medline: 18 7 2020
entrez: 1 10 2019
Statut: ppublish

Résumé

8-oxo-7,8-dihydroguanine, commonly referred to as 8-oxoG, is considered one of the most predominant oxidative lesions formed in DNA. Due to its ability to pair with adenines in its syn configuration, this lesion has a strong mutagenic potential in both eukaryotes and prokaryotes. Escherichia coli cells are endowed with the GO system, which protects them from the mutagenic properties of this lesion when formed both in cellular DNA and the nucleotide pool. MutY and MutM (Fpg) DNA glycosylases are crucial components of the GO system. A strong mutator phenotype of the Escherichia coli mutM mutY double mutant underscores the importance of 8-oxoG repair for genomic stability. Here, we report that in Caulobacter crescentus, a widely studied alpha-proteobacterium with a GC-rich genome, the combined lack of MutM and MutY glycosylases produces a more modest mutator phenotype when compared to E. coli. Genetic analysis indicates that other glycosylases and other repair pathways do not act synergistically with the GO system for spontaneous mutation prevention. We also show that there is not a statistically significant difference in the spontaneous levels 8-oxodGuo in E. coli and C. crescentus, suggesting that other yet to be identified differences in repair or replication probably account for the differential importance of the GO system between these two species. Environ. Mol. Mutagen. 61:246-255, 2020. © 2019 Wiley Periodicals, Inc.

Identifiants

pubmed: 31569269
doi: 10.1002/em.22335
doi:

Substances chimiques

Bacterial Proteins 0
DNA, Bacterial 0
Escherichia coli Proteins 0
8-hydroxyguanine 5614-64-2
Guanine 5Z93L87A1R
DNA Glycosylases EC 3.2.2.-
mutY adenine glycosylase EC 3.2.2.-
DNA-Formamidopyrimidine Glycosylase EC 3.2.2.23
DNA-formamidopyrimidine glycosylase, E coli EC 3.2.2.23

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

246-255

Subventions

Organisme : Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
ID : 2014/15982-6
Pays : International
Organisme : Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
ID : 2009/51387-7
Pays : International
Organisme : Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
ID : CEPID-Redoxoma 2013/07937-8
Pays : International
Organisme : Coordenação de Aperfeiçoamento de Pessoal de Nível Superior-Brasil (CAPES)-Finance Code 001
Pays : International

Informations de copyright

© 2019 Wiley Periodicals, Inc.

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Auteurs

Frank S Fernández-Silva (FS)

Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, SP, Brazil.

Mariane L Schulz (ML)

Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo, SP, Brazil.

Ingrid Reale Alves (IR)

Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, SP, Brazil.

Rubia R Freitas (RR)

Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, SP, Brazil.

Raquel Paes da Rocha (RP)

Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, SP, Brazil.

Carina O Lopes-Kulishev (CO)

Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, SP, Brazil.

Marisa H G Medeiros (MHG)

Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo, SP, Brazil.

Rodrigo S Galhardo (RS)

Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, SP, Brazil.

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