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Microbiology. 2017 Jul;163(7):1016-1029. doi: 10.1099/mic.0.000489. Epub 2017 Jul 21.

DprA from Neisseria meningitidis: properties and role in natural competence for transformation.

Author information

1
1​Department of Microbiology, University of Oslo, Oslo, Norway †​Present address: Lovisenberg Diaconal Hospital, Oslo, Norway.
2
1​Department of Microbiology, University of Oslo, Oslo, Norway.
3
2​Department of Microbiology, Oslo University Hospital, Oslo, Norway.
4
3​Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, University of Manchester, Oxford Road, Manchester, UK.
5
2​Department of Microbiology, Oslo University Hospital, Oslo, Norway 1​Department of Microbiology, University of Oslo, Oslo, Norway.
6
2​Department of Microbiology, Oslo University Hospital, Oslo, Norway ‡​Present address: Department of Life Sciences and Health, Oslo and Akershus University College of Applied Sciences, Norway.

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.

PMID:
28696187
PMCID:
PMC5817196
DOI:
10.1099/mic.0.000489
[Indexed for MEDLINE]
Free PMC Article

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