ArticleJournal of bacteriology2008
Enterococcus faecalis PcfC, a spatially localized substrate receptor for type IV secretion of the pCF10 transfer intermediate.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Article
- Article
- Structural foundation for the role of enterococcal PrgB in conjugation, biofilm formation, and virulence.eLife · 2023Article
- Characterization of ConE, the VirB4 Homolog of the Integrative and Conjugative Element ICEJournal of bacteriology · 2023Article
- Group II Introns Generate Functional Chimeric Relaxase Enzymes with Modified Specificities through Exon Shuffling at Both the RNA and DNA Level.Molecular biology and evolution · 2021Article
- Ratiometric quorum sensing governs the trade-off between bacterial vertical and horizontal antibiotic resistance propagation.PLoS biology · 2020Article
- The TraK accessory factor activates substrate transfer through the pKM101 type IV secretion system independently of its role in relaxosome assembly.Molecular microbiology · 2020Article
- Prevalence of an Intestinal ST40International journal of molecular sciences · 2020Article
- Competent but complex communication: The phenomena of pheromone-responsive plasmids.PLoS pathogens · 2020Review
- Type IV Coupling Proteins as Potential Targets to Control the Dissemination of Antibiotic Resistance.Frontiers in molecular biosciences · 2020Review
- Conjugative Coupling Proteins and the Role of Their Domains in Conjugation, Secondary Structure andFrontiers in molecular biosciences · 2020Article
- Inhibiting bacterial secretion systems in the fight against antibiotic resistance.MedChemComm · 2019Review
- Enterococcal Genetics.Microbiology spectrum · 2019Review
- Enterococcal PcfF Is a Ribbon-Helix-Helix Protein That Recruits the Relaxase PcfG Through Binding and Bending of theFrontiers in microbiology · 2019Article
- PrgB promotes aggregation, biofilm formation, and conjugation through DNA binding and compaction.Molecular microbiology · 2018Article
- Substrate translocation involves specific lysine residues of the central channel of the conjugative coupling protein TrwB.Molecular genetics and genomics : MGG · 2017Article
- PrgU: a suppressor of sex pheromone toxicity in Enterococcus faecalis.Molecular microbiology · 2017Article
- TheFrontiers in microbiology · 2017Article
- Rampant Parasexuality Evolves in a Hospital Pathogen during Antibiotic Selection.Molecular biology and evolution · 2015Article
- Critical Components of the Conjugation Machinery of the Integrative and Conjugative Element ICEBs1 of Bacillus subtilis.Journal of bacteriology · 2015Article
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Authors and funding
6 authors.
Funding
Abstract
Upon sensing of peptide pheromone, Enterococcus faecalis efficiently transfers plasmid pCF10 through a type IV secretion (T4S) system to recipient cells. The PcfF accessory factor and PcfG relaxase initiate transfer by catalyzing strand-specific nicking at the pCF10 origin of transfer sequence (oriT). Here, we present evidence that PcfF and PcfG spatially coordinate docking of the pCF10 transfer intermediate with PcfC, a membrane-bound putative ATPase related to the coupling proteins of gram-negative T4S machines. PcfC and PcfG fractionated with the membrane and PcfF with the cytoplasm, yet all three proteins formed several punctate foci at the peripheries of pheromone-induced cells as monitored by immunofluorescence microscopy. A PcfC Walker A nucleoside triphosphate (NTP) binding site mutant (K156T) fractionated with the E. faecalis membrane and also formed foci, whereas PcfC deleted of its N-terminal putative transmembrane domain (PcfCDelta N103) distributed uniformly throughout the cytoplasm. Native PcfC and mutant proteins PcfCK156T and PcfCDelta N103 bound pCF10 but not pcfG or Delta oriT mutant plasmids as shown by transfer DNA immunoprecipitation, indicating that PcfC binds only the processed form of pCF10 in vivo. Finally, purified PcfCDelta N103 bound DNA substrates and interacted with purified PcfF and PcfG in vitro. Our findings support a model in which (i) PcfF recruits PcfG to oriT to catalyze T-strand nicking, (ii) PcfF and PcfG spatially position the relaxosome at the cell membrane to stimulate substrate docking with PcfC, and (iii) PcfC initiates substrate transfer through the pCF10 T4S channel by an NTP-dependent mechanism.
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