ArticleJournal of bacteriology2011
TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 20 citations in OpenAlex.
- Genome-wide characterization of host factors involved in single-stranded RNA and DNA phage infection pathways.bioRxiv : the preprint server for biology · 2026Article
- Chimeric systems composed of swapped Tra subunits between distantly-related F plasmids reveal striking plasticity among type IV secretion machines.PLoS genetics · 2024Article
- 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
- Chimeric systems composed of swapped Tra subunits between distantly-related F plasmids reveal striking plasticity among type IV secretion machines.bioRxiv : the preprint server for biology · 2023Article
- Conjugation's Toolkit: the Roles of Nonstructural Proteins in Bacterial Sex.Journal of bacteriology · 2023Review
- Contributions of F-specific subunits to the F plasmid-encoded type IV secretion system and F pilus.Molecular microbiology · 2022Article
- Article
- Protein Dynamics in F-like Bacterial Conjugation.Biomedicines · 2020Review
- Aeropyrum pernix membrane topology of protein VKOR promotes protein disulfide bond formation in two subcellular compartments.Microbiology (Reading, England) · 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
- Dynactin integrity depends upon direct binding of dynamitin to Arp1.Molecular biology of the cell · 2014Article
- The multidrug resistance IncA/C transferable plasmid encodes a novel domain-swapped dimeric protein-disulfide isomerase.The Journal of biological chemistry · 2014Article
- Review
- The interplay between the disulfide bond formation pathway and cytochrome c maturation in Escherichia coli.FEBS letters · 2012Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
TrbB, a periplasmic protein encoded by the conjugative plasmid F, has a predicted thioredoxin-like fold and possesses a C-X-X-C redox active site motif. TrbB may function in the conjugative process by serving as a disulfide bond isomerase, facilitating proper folding of a subset of F-plasmid-encoded proteins in the periplasm. Previous studies have demonstrated that a ΔtrbB F plasmid in Escherichia coli lacking DsbC(E.coli), its native disulfide bond isomerase, experiences a 10-fold decrease in mating efficiency but have not provided direct evidence for disulfide bond isomerase activity. Here we demonstrate that trbB can partially restore transfer of a variant of the distantly related R27 plasmid when both chromosomal and plasmid genes encoding disulfide bond isomerases have been disrupted. In addition, we show that TrbB displays both disulfide bond isomerase and reductase activities on substrates not involved in the conjugative process. Unlike canonical members of the disulfide bond isomerase family, secondary structure predictions suggest that TrbB lacks both an N-terminal dimerization domain and an α-helical domain found in other disulfide bond isomerases. Phylogenetic analyses support the conclusion that TrbB belongs to a unique family of plasmid-based disulfide isomerases. Interestingly, although TrbB diverges structurally from other disulfide bond isomerases, we show that like those isomerases, TrbB relies on DsbD from E. coli for maintenance of its C-X-X-C redox active site motif.
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