ArticleMicrobiology (Reading, England)2017
DprA from Neisseria meningitidis: properties and role in natural competence for transformation.
Article in Microbiology (Reading, England), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- A Single DNA Binding Site of DprA Dimer Is Required to Facilitate RecA Filament Nucleation.International journal of molecular sciences · 2025Article
- Structure and functions of a multireplicon genome of Antarctic Psychrobacter sp. ANT_H3: characterization of the genetic modules suitable for the construction of the plasmid-vectors for cold-active bacteria.Journal of applied genetics · 2023Article
- Natural Transformation ofFrontiers in microbiology · 2021Article
- Targeting evolution of antibiotic resistance by SOS response inhibition.Computational and structural biotechnology journal · 2021Review
- Synergic Effects of Temperature and Irradiance on the Physiology of the MarineFrontiers in microbiology · 2020Article
- The Lonely Guy (LOG) Homologue SiRe_0427 from the Thermophilic ArchaeonApplied and environmental microbiology · 2019Article
- Article
- DprA Is Essential for Natural Competence inFrontiers in genetics · 2019Article
- A genomic view of experimental intraspecies and interspecies transformation of a rifampicin-resistance allele into Neisseria meningitidis.Microbial genomics · 2018Article
- Pull in and Push Out: Mechanisms of Horizontal Gene Transfer in Bacteria.Frontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA processing chain A (DprA) is a DNA-binding protein that is ubiquitous in bacteria and expressed in some archaea. DprA is active in many bacterial species that are competent for transformation of DNA, but its role in Neisseriameningitidis (Nm) is not well characterized. An Nm mutant lacking DprA was constructed, and the phenotypes of the wild-type and ΔdprA mutant were compared. The salient feature of the phenotype of dprA null cells is the total lack of competence for genetic transformation shown by all of the donor DNA substrates tested in this study. Here, Nm wild-type and dprA null cells appeared to be equally resistant to genotoxic stress. The gene encoding DprANm was cloned and overexpressed, and the biological activities of DprANm were further investigated. DprANm binds ssDNA more strongly than dsDNA, but lacks DNA uptake sequence-specific DNA binding. DprANm dimerization and interaction with the C-terminal part of the single-stranded binding protein SSBNmwere demonstrated. dprA is co-expressed with smg, a downstream gene of unknown function, and the gene encoding topoisomerase 1, topA.
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