ArticleMicrobiologyOpen2017
Mechanisms of peptide sex pheromone regulation of conjugation in Enterococcus faecalis.
Article in MicrobiologyOpen, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 29 citations in OpenAlex.
- Bacterial quorum-sensing systems in cell-cell communication.FEMS microbiology reviews · 2026Review
- A newly discoveredFrontiers in microbiology · 2026Article
- Factors affecting CRISPR-Cas defense against antibiotic resistance plasmids harboured byMicrobiology (Reading, England) · 2025Article
- Pheromone cCF10 inhibits the antibiotic persistence ofFrontiers in microbiology · 2024Article
- Structural Differences in Complexes between the Master Regulator PrgX, Peptide Pheromones, and Operator Binding Sites Determine the Induction State for Conjugative Transfer of pCF10.Journal of bacteriology · 2022Article
- Pheromone Activity after Stimulation with Ampicillin in a Plasmid-FreeMicroorganisms · 2022Article
- Let Me Upgrade You: Impact of Mobile Genetic Elements on Enterococcal Adaptation and Evolution.Journal of bacteriology · 2021Review
- Two ABC transport systems carry out peptide uptake in Enterococcus faecalis: Their roles in growth and in uptake of sex pheromones.Molecular microbiology · 2021Article
- Quorum sensing for population-level control of bacteria and potential therapeutic applications.Cellular and molecular life sciences : CMLS · 2020Review
- Competent but complex communication: The phenomena of pheromone-responsive plasmids.PLoS pathogens · 2020Review
- Single-Cell Analysis Reveals that the Enterococcal Sex Pheromone Response Results in Expression of Full-Length Conjugation Operon Transcripts in All Induced Cells.Journal of bacteriology · 2020Article
- Antibacterial of Dibenzo-Drug design, development and therapy · 2020Article
- Exposure to One Antibiotic Leads to Acquisition of Resistance to Another AntibioticFrontiers in microbiology · 2020Article
- Effects of endogenous levels of master regulator PrgX and peptide pheromones on inducibility of conjugation in the enterococcal pCF10 system.Molecular microbiology · 2019Article
- Multiplex PCR analysis of virulence genes and their influence on antibiotic resistance inJournal of veterinary science · 2019Article
- Enterococcal Genetics.Microbiology spectrum · 2019Review
- Regulation of Gram-Positive Conjugation.Frontiers in microbiology · 2019Review
- Biofilm-associated infection by enterococci.Nature reviews. Microbiology · 2019Review
- Mechanistic Features of the Enterococcal pCF10 Sex Pheromone Response and the Biology of Enterococcus faecalis in Its Natural Habitat.Journal of bacteriology · 2018Review
- A novel chemical inducer ofThe Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
In many gram positive bacteria, horizontal transfer and virulence are regulated by peptide-mediated cell-cell signaling. The heptapeptide cCF10 (C) activates conjugative transfer of the Enterococcus faecalis plasmid pCF10, whereas the iCF10 (I) peptide inhibits transfer. Both peptides bind to the same domain of the master transcription regulator PrgX, a repressor of transcription of the prgQ operon encoding conjugation genes. We show that repression of prgQ by PrgX tetramers requires formation of a pCF10 DNA loop where each of two PrgX DNA-binding sites is occupied by a dimer. I binding to PrgX enhances prgQ repression, while C binding has the opposite effect. Previous models suggested that differential effects of these two peptides on the PrgX oligomerization state accounted for their distinct functions. Our new results demonstrate that both peptides have similar, high-binding affinity for PrgX, and that both peptides actually promote formation of PrgX tetramers with higher DNA-binding affinity than Apo-PrgX. We propose that differences in repression ability of PrgX/peptide complexes result from subtle differences in the structures of DNA-bound PrgX/peptide complexes. Changes in the induction state of a donor cell likely results from replacement of one type of DNA-bound peptide/PrgX tetramer with the other.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.