ArticleJournal of bacteriology2003
TraG-like proteins of type IV secretion systems: functional dissection of the multiple activities of TraG (RP4) and TrwB (R388).
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 89 citations in OpenAlex.
- TraN variants mediate conjugation species specificity of IncA/C, IncH, andJournal of bacteriology · 2026Article
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- Host defense peptides mitigate the spread of antibiotic resistance in physiologically relevant condition.Antimicrobial agents and chemotherapy · 2024Article
- Surface Plasmon Resonance: A Sensitive Tool to Study Protein-Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2024Article
- VirB4- and VirD4-Like ATPases, Components of a Putative Type 4C Secretion System in Clostridioides difficile.Journal of bacteriology · 2021Article
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- Genome-wide insights into population structure and host specificity of Campylobacter jejuni.Scientific reports · 2021Article
- Plasmid Transfer by Conjugation in Gram-Negative Bacteria: From the Cellular to the Community Level.Genes · 2020Review
- Conjugative Coupling Proteins and the Role of Their Domains in Conjugation, Secondary Structure andFrontiers in molecular biosciences · 2020Article
- Transcriptome Analysis of Zygotic Induction During Conjugative Transfer of Plasmid RP4.Frontiers in microbiology · 2020Article
- Type IV Coupling Proteins as Potential Targets to Control the Dissemination of Antibiotic Resistance.Frontiers in molecular biosciences · 2020Review
- Article
- 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
- Hotspot mutations and ColE1 plasmids contribute to the fitness of Salmonella Heidelberg in poultry litter.PloS one · 2018Article
- 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
- Social behavior and decision making in bacterial conjugation.Frontiers in cellular and infection microbiology · 2014Review
- Structure of a translocation signal domain mediating conjugative transfer by type IV secretion systems.Molecular microbiology · 2013Article
- Enterococcus faecalis PrgJ, a VirB4-like ATPase, mediates pCF10 conjugative transfer through substrate binding.Journal of bacteriology · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TraG-like proteins are essential components of type IV secretion systems. During secretion, TraG is thought to translocate defined substrates through the inner cell membrane. The energy for this transport is presumably delivered by its potential nucleotide hydrolase (NTPase) activity. TraG of conjugative plasmid RP4 is a membrane-anchored oligomer that binds RP4 relaxase and DNA. TrwB (R388) is a hexameric TraG-like protein that binds ATP. Both proteins, however, lack NTPase activity under in vitro conditions. We characterized derivatives of TraG and TrwB truncated by the N-terminal membrane anchor (TraGdelta2 and TrwBdelta1) and/or containing a point mutation at the putative nucleotide-binding site (TraGdelta2K187T and TraGK187T). Unlike TraG and TrwB, truncated derivatives behaved as monomers without the tendency to form oligomers or aggregates. Surface plasmon resonance analysis with immobilized relaxase showed that mutant TraGK187T was as good a binding partner as the wild-type protein, whereas truncated TraG monomers were unable to bind relaxase. TraGdelta2 and TrwBdelta1 bound ATP and, with similar affinity, ADP. Binding of ATP and ADP was strongly inhibited by the presence of Mg(2+) or single-stranded DNA and was competed for by other nucleotides. Compared to the activity of TraGdelta2, the ATP- and ADP-binding activity of the point mutation derivative TraGdelta2K187T was significantly reduced. Each TraG derivative bound DNA with an affinity similar to that of the native protein. DNA binding was inhibited or competed for by ATP, ADP, and, most prominently, Mg(2+). Thus, both nucleotide binding and DNA binding were sensitive to Mg(2+) and were competitive with respect to each other.
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