ArticleJournal of bacteriology2013
Neisseria gonorrhoeae RecQ helicase HRDC domains are essential for efficient binding and unwinding of the pilE guanine quartet structure required for pilin antigenic variation.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- G-quadruplex DNA: a novel target for drug design.Cellular and molecular life sciences : CMLS · 2021Review
- The HRDC domain oppositely modulates the unwinding activity of E. coli RecQ helicase on duplex DNA and G-quadruplex.The Journal of biological chemistry · 2020Article
- Altering theBiochemistry · 2020Article
- Antigenic Variation inJournal of bacteriology · 2020Article
- Changing of the guard: How the Lyme disease spirochete subverts the host immune response.The Journal of biological chemistry · 2020Review
- Transcriptional initiation of a small RNA, not R-loop stability, dictates the frequency of pilin antigenic variation in Neisseria gonorrhoeae.Molecular microbiology · 2019Article
- Guanine Quadruplex DNA Regulates Gamma Radiation Response of Genome Functions in the Radioresistant BacteriumJournal of bacteriology · 2019Article
- A Double-Strand Break Does Not Promote Neisseria gonorrhoeae Pilin Antigenic Variation.Journal of bacteriology · 2019Article
- Characterization of highly conserved G-quadruplex motifs as potential drug targets in Streptococcus pneumoniae.Scientific reports · 2019Article
- Analysis of Pilin Antigenic Variation in Neisseria meningitidis by Next-Generation Sequencing.Journal of bacteriology · 2018Article
- A guanine-flipping and sequestration mechanism for G-quadruplex unwinding by RecQ helicases.Nature communications · 2018Article
- Initiation of homologous recombination at DNA nicks.Nucleic acids research · 2018Review
- Mapping and characterization of G-quadruplexes in Mycobacterium tuberculosis gene promoter regions.Scientific reports · 2017Article
- Does DNA replication direct locus-specific recombination during host immune evasion by antigenic variation in the African trypanosome?Current genetics · 2017Review
- Analyzing Neisseria gonorrhoeae Pilin Antigenic Variation Using 454 Sequencing Technology.Journal of bacteriology · 2016Article
- Neisseria gonorrhoeae MutS affects pilin antigenic variation through mismatch correction and not by pilE guanine quartet binding.Journal of bacteriology · 2015Article
- Mobile DNA in the pathogenicMicrobiology spectrum · 2015Article
- G-quadruplexes in pathogens: a common route to virulence control?PLoS pathogens · 2015Review
- Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures.Nature communications · 2014Article
- The intrinsically disordered amino-terminal region of human RecQL4: multiple DNA-binding domains confer annealing, strand exchange and G4 DNA binding.Nucleic acids research · 2014Article
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5 authors.
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Abstract
The strict human pathogen Neisseria gonorrhoeae utilizes homologous recombination to antigenically vary the pilus, thus evading the host immune response. High-frequency gene conversion reactions between many silent pilin loci and the expressed pilin locus (pilE) allow for numerous pilus variants per strain to be produced from a single strain. For pilin antigenic variation (Av) to occur, a guanine quartet (G4) structure must form upstream of pilE. The RecQ helicase is one of several recombination or repair enzymes required for efficient levels of pilin Av, and RecQ family members have been shown to bind to and unwind G4 structures. Additionally, the vast majority of RecQ helicase family members encode one "helicase and RNase D C-terminal" (HRDC) domain, whereas the N. gonorrhoeae RecQ helicase gene encodes three HRDC domains, which are critical for pilin Av. Here, we confirm that deletion of RecQ HRDC domains 2 and 3 causes a decrease in the frequency of pilin Av comparable to that obtained with a functional knockout. We demonstrate that the N. gonorrhoeae RecQ helicase can bind and unwind the pilE G4 structure. Deletion of the RecQ HRDC domains 2 and 3 resulted in a decrease in G4 structure binding and unwinding. These data suggest that the decrease in pilin Av observed in the RecQ HRDC domain 2 and 3 deletion mutant is a result of the enzyme's inability to efficiently bind and unwind the pilE G4 structure.
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