ArticlePloS one2011
Purification and characterization of the RecA protein from Neisseria gonorrhoeae.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
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- Put your money where your mouth is: Surveillance of antibiotic resistance within the commensalbioRxiv : the preprint server for biology · 2026Article
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- A genomic view of experimental intraspecies and interspecies transformation of a rifampicin-resistance allele into Neisseria meningitidis.Microbial genomics · 2018Article
- RNA markers enable phenotypic test of antibiotic susceptibility in Neisseria gonorrhoeae after 10 minutes of ciprofloxacin exposure.Scientific reports · 2018Article
- Article
- Article
- P1 Ref Endonuclease: A Molecular Mechanism for Phage-Enhanced Antibiotic Lethality.PLoS genetics · 2016Article
- Mobile DNA in the pathogenicMicrobiology spectrum · 2015Article
- Biochemical characterization of RecA variants that contribute to extreme resistance to ionizing radiation.DNA repair · 2015Article
- RecA-binding pilE G4 sequence essential for pilin antigenic variation forms monomeric and 5' end-stacked dimeric parallel G-quadruplexes.Structure (London, England : 1993) · 2012Article
- Characterization of the single stranded DNA binding protein SsbB encoded in the Gonoccocal Genetic Island.PloS one · 2012Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The strict human pathogen Neisseria gonorrhoeae is the only causative agent of the sexually transmitted infection gonorrhea. The recA gene from N. gonorrhoeae is essential for DNA repair, natural DNA transformation, and pilin antigenic variation, all processes that are important for the pathogenesis and persistence of N. gonorrhoeae in the human population. To understand the biochemical features of N. gonorrhoeae RecA (RecA(Ng)), we overexpressed and purified the RecA(Ng) and SSB(Ng) proteins and compared their activities to those of the well-characterized E. coli RecA and SSB proteins in vitro. We observed that RecA(Ng) promoted more strand exchange at early time points than RecA(Ec) through DNA homologous substrates, and exhibited the highest ATPase activity of any RecA protein characterized to date. Further analysis of this robust ATPase activity revealed that RecA(Ng) is more efficient at displacing SSB from ssDNA and that RecA(Ng) shows higher ATPase activity during strand exchange than RecA(Ec). Using substrates created to mimic the cellular processes of DNA transformation and pilin antigenic variation we observed that RecA(Ec) catalyzed more strand exchange through a 100 bp heterologous insert, but that RecA(Ng) catalyzed more strand exchange through regions of microheterology. Together, these data suggest that the processes of ATP hydrolysis and DNA strand exchange may be coupled differently in RecA(Ng) than in RecA(Ec). This difference may explain the unusually high ATPase activity observed for RecA(Ng) with the strand exchange activity between RecA(Ng) and RecA(Ec) being more similar.
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Registered trials
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