ArticleJournal of bacteriology2010
Functional dissection of the conjugative coupling protein TrwB.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Article
- Type IV secretion systems: from structures to mechanisms.The EMBO journal · 2025Review
- DNA Transport through the Dynamic Type IV Secretion System.Infection and immunity · 2023Review
- Characterization of ConE, the VirB4 Homolog of the Integrative and Conjugative Element ICEJournal of bacteriology · 2023Article
- Mechanism of regulation of the Helicobacter pylori Cagβ ATPase by CagZ.Nature communications · 2023Article
- Article
- Article
- Conjugative Coupling Proteins and the Role of Their Domains in Conjugation, Secondary Structure andFrontiers in molecular biosciences · 2020Article
- Type IV Coupling Proteins as Potential Targets to Control the Dissemination of Antibiotic Resistance.Frontiers in molecular biosciences · 2020Review
- Development of TEM-1 β-lactamase based protein translocation assay for identification of Anaplasma phagocytophilum type IV secretion system effector proteins.Scientific reports · 2019Article
- Biological and Structural Diversity of Type IV Secretion Systems.Microbiology spectrum · 2019Review
- Structure of a VirD4 coupling protein bound to a VirB type IV secretion machinery.The EMBO journal · 2017Article
- Substrate translocation involves specific lysine residues of the central channel of the conjugative coupling protein TrwB.Molecular genetics and genomics : MGG · 2017Article
- Identification of oriT and a recombination hot spot in the IncA/C plasmid backbone.Scientific reports · 2017Article
- DNA Delivery and Genomic Integration into Mammalian Target Cells through Type IV A and B Secretion Systems of Human Pathogens.Frontiers in microbiology · 2017Article
- Chimeric Coupling Proteins Mediate Transfer of Heterologous Type IV Effectors through the Escherichia coli pKM101-Encoded Conjugation Machine.Journal of bacteriology · 2016Article
- The Mosaic Type IV Secretion Systems.EcoSal Plus · 2016Review
- Critical Components of the Conjugation Machinery of the Integrative and Conjugative Element ICEBs1 of Bacillus subtilis.Journal of bacteriology · 2015Article
- The All-Alpha Domains of Coupling Proteins from the Agrobacterium tumefaciens VirB/VirD4 and Enterococcus faecalis pCF10-Encoded Type IV Secretion Systems Confer Specificity to Binding of Cognate DNA Substrates.Journal of bacteriology · 2015Article
- Chloramphenicol Selection of IS10 Transposition in the cat Promoter Region of Widely Used Cloning Vectors.PloS one · 2015Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The conjugative coupling protein TrwB is responsible for connecting the relaxosome to the type IV secretion system during conjugative DNA transfer of plasmid R388. It is directly involved in transport of the relaxase TrwC, and it displays an ATPase activity probably involved in DNA pumping. We designed a conjugation assay in which the frequency of DNA transfer is directly proportional to the amount of TrwB. A collection of point mutants was constructed in the TrwB cytoplasmic domain on the basis of the crystal structure of TrwB Delta N70, targeting the nucleotide triphosphate (NTP)-binding region, the cytoplasmic surface, or the internal channel in the hexamer. An additional set of transfer-deficient mutants was obtained by random mutagenesis. Most mutants were impaired in both DNA and protein transport. We found that the integrity of the nucleotide binding domain is absolutely required for TrwB function, which is also involved in monomer-monomer interactions. Polar residues surrounding the entrance and inside the internal channel were important for TrwB function and may be involved in interactions with the relaxosomal components. Finally, the N-terminal transmembrane domain of TrwB was subjected to random mutagenesis followed by a two-hybrid screen for mutants showing enhanced protein-protein interactions with the related TrwE protein of Bartonella tribocorum. Several point mutants were obtained with mutations in the transmembranal helices: specifically, one proline from each protein may be the key residue involved in the interaction of the coupling protein with the type IV secretion apparatus.
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