ArticleJournal of bacteriology2009
The pentapeptide repeat proteins MfpAMt and QnrB4 exhibit opposite effects on DNA gyrase catalytic reactions and on the ternary gyrase-DNA-quinolone complex.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 57 citations in OpenAlex.
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- Comparative genomics of the Neodiprion sertifer nucleopolyhedrovirus from Turkey with the fewest ORFs among baculoviruses.Virus genes · 2024Article
- Friend or Foe: Protein Inhibitors of DNA Gyrase.Biology · 2024Review
- Comprehensive profile of the companion animal gut microbiome integrating reference-based and reference-free methods.The ISME journal · 2024Article
- Metagenome diversity illuminates origins of pathogen effectors.bioRxiv : the preprint server for biology · 2023Article
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- Escherichia coli GyrA Tower Domain Interacts with QnrB1 Loop B and Plays an Important Role in QnrB1 Protection from Quinolone Inhibition.Antimicrobial agents and chemotherapy · 2021Article
- The pentapeptide-repeat protein, MfpA, interacts with mycobacterial DNA gyrase as a DNA T-segment mimic.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Pentapeptide repeat protein QnrB1 requires ATP hydrolysis to rejuvenate poisoned gyrase complexes.Nucleic acids research · 2021Article
- Overexpression ofInternational journal of microbiology · 2021Article
- Mobilome and Resistome Reconstruction from Genomes Belonging to Members of theMicroorganisms · 2019Article
- The Microbial Toxin Microcin B17: Prospects for the Development of New Antibacterial Agents.Journal of molecular biology · 2019Review
- The plasmid-borne quinolone resistance protein QnrB, a novel DnaA-binding protein, increases the bacterial mutation rate by triggering DNA replication stress.Molecular microbiology · 2019Article
- Kctd9 Deficiency Impairs Natural Killer Cell Development and Effector Function.Frontiers in immunology · 2019Article
- Interference with KCTD9 inhibits NK cell activation and ameliorates fulminant liver failure in mice.BMC immunology · 2018Article
- DNA Replication in Mycobacterium tuberculosis.Microbiology spectrum · 2017Review
- Comparative analysis of an IncR plasmid carrying armA, blaDHA-1 and qnrB4 from Klebsiella pneumoniae ST37 isolates.The Journal of antimicrobial chemotherapy · 2016Article
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MfpA(Mt) and QnrB4 are two newly characterized pentapeptide repeat proteins (PRPs) that interact with DNA gyrase. The mfpA(Mt) gene is chromosome borne in Mycobacterium tuberculosis, while qnrB4 is plasmid borne in enterobacteria. We expressed and purified the two PRPs and compared their effects on DNA gyrase, taking into account host specificity, i.e., the effect of MfpA(Mt) on M. tuberculosis gyrase and the effect of QnrB4 on Escherichia coli gyrase. Whereas QnrB4 inhibited E. coli gyrase activity only at concentrations higher than 30 microM, MfpA(Mt) inhibited all catalytic reactions of the M. tuberculosis gyrase described for this enzyme (supercoiling, cleavage, relaxation, and decatenation) with a 50% inhibitory concentration of 2 microM. We showed that the D87 residue in GyrA has a major role in the MfpA(Mt)-gyrase interaction, as D87H and D87G substitutions abolished MfpA(Mt) inhibition of M. tuberculosis gyrase catalytic reactions, while A83S modification did not. Since MfpA(Mt) and QnrB4 have been involved in resistance to fluoroquinolones, we measured the inhibition of the quinolone effect in the presence of each PRP. QnrB4 reversed quinolone inhibition of E. coli gyrase at 0.1 microM as described for other Qnr proteins, but MfpA(Mt) did not modify M. tuberculosis gyrase inhibition by fluoroquinolones. Crossover experiments showed that MfpA(Mt) also inhibited E. coli gyrase function, while QnrB4 did not reverse quinolone inhibition of M. tuberculosis gyrase. In conclusion, our in vitro experiments showed that MfpA(Mt) and QnrB4 exhibit opposite effects on DNA gyrase and that these effects are protein and species specific.
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