ArticleJournal of bacteriology2005
F-like type IV secretion systems encode proteins with thioredoxin folds that are putative DsbC homologues.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- A comprehensive list of genes required for the efficient conjugation of plasmid Rts1 was determined by systematic deletion analysis.DNA research : an international journal for rapid publication of reports on genes and genomes · 2024Article
- Structural insights into the disulfide isomerase and chaperone activity of TrbB of the F plasmid type IV secretion system.Current research in structural biology · 2024Article
- Article
- Conjugation's Toolkit: the Roles of Nonstructural Proteins in Bacterial Sex.Journal of bacteriology · 2023Review
- Characterization of an atypical but widespread type IV secretion system for transfer of the integrative and conjugative element (ICEclc) in Pseudomonas putida.Nucleic acids research · 2023Article
- Contributions of F-specific subunits to the F plasmid-encoded type IV secretion system and F pilus.Molecular microbiology · 2022Article
- Protein interactions within and between two F-type type IV secretion systems.Molecular microbiology · 2020Article
- Protein Dynamics in F-like Bacterial Conjugation.Biomedicines · 2020Review
- Temperature Dependent Control of the R27 Conjugative Plasmid Genes.Frontiers in molecular biosciences · 2020Article
- Conjugative Mating Assays for Sequence-specific Analysis of Transfer Proteins Involved in Bacterial Conjugation.Journal of visualized experiments : JoVE · 2017Article
- Chemical shift assignments of a reduced N-terminal truncation mutant of the disulfide bond isomerase TrbB from plasmid F, TrbBΔ29.Biomolecular NMR assignments · 2014Article
- The multidrug resistance IncA/C transferable plasmid encodes a novel domain-swapped dimeric protein-disulfide isomerase.The Journal of biological chemistry · 2014Article
- Review
- TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance.Journal of bacteriology · 2011Article
- F plasmid TraF and TraH are components of an outer membrane complex involved in conjugation.Journal of bacteriology · 2010Article
- Comparative ICE genomics: insights into the evolution of the SXT/R391 family of ICEs.PLoS genetics · 2009Article
- Arabidopsis INOSITOL TRANSPORTER2 mediates H+ symport of different inositol epimers and derivatives across the plasma membrane.Plant physiology · 2007Article
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
F and R27 are conjugative plasmids of enteric bacteria belonging to the IncF and IncHI1 plasmid incompatibility groups, respectively. Based on sequence analysis, two genes of the F transfer region, traF and trbB, and three genes of the R27 transfer region, trhF, dsbC, and htdT, are predicted to encode periplasmic proteins containing a C-terminal thioredoxin fold. The C-X-X-C active-site motif of thioredoxins is present in all of these proteins except TraF(F). Escherichia coli carrying a dsbA mutation, which is deficient in disulfide bond formation, cannot synthesize pili and exhibits hypersensitivity to dithiothreitol (DTT) as monitored by mating ability. Overproduction of the E. coli disulfide bond isomerase DsbC, TrbB(F), DsbC(R27), or HtdT(R27), but not TraF(F) or TrhF(R27), reverses this hypersensitivity to DTT. Site-directed mutagenesis established that the C-X-X-C motif was necessary for this activity. Secretion into the periplasm of the C-terminal regions of TrbB(F) and DsbC(R27), containing putative thioredoxin folds, but not TrhF(R27), partially complemented the host dsbA mutation. A trbB(F) deletion mutant showed a 10-fold-lower mating efficiency in an E. coli dsbC null strain but had no phenotype in wild-type E. coli, suggesting redundancy in function between TrbB(F) and E. coli DsbC. Our results indicate that TrbB(F), DsbC(R27), and HtdT(R27) are putative disulfide bond isomerases for their respective transfer systems. TraF(F) is essential for conjugation but appears to have a function other than disulfide bond chemistry.
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