ArticleJournal of molecular biology2004
Agrobacterium tumefaciens VirB6 domains direct the ordered export of a DNA substrate through a type IV secretion System.
Article in Journal of molecular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed.
- Article
- Inner membrane components of the plasmid pKM101 type IV secretion system TraE and TraD are DNA-binding proteins.Scientific reports · 2025Article
- Article
- Structural and functional diversity of type IV secretion systems.Nature reviews. Microbiology · 2024Review
- Probing Protein Topology and Conformation by Limited Proteolysis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Evolution and exchange of plasmids in pathogenicmSphere · 2023Article
- Cryo-EM structure of the Agrobacterium tumefaciens T4SS-associated T-pilus reveals stoichiometric protein-phospholipid assembly.Structure (London, England : 1993) · 2023Article
- 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
- Disruption of VirB6 Paralogs in Anaplasma phagocytophilum Attenuates Its Growth.Journal of bacteriology · 2020Article
- Development of PCR-Based Molecular Marker for Detection ofThe plant pathology journal · 2020Article
- Comparative Genomic Analysis Confirms Five Genetic Populations of the Select Agent,Microorganisms · 2020Article
- Identification, characterization and benefits of an exclusion system in an integrative and conjugative element of Bacillus subtilis.Molecular microbiology · 2019Article
- Biological and Structural Diversity of Type IV Secretion Systems.Microbiology spectrum · 2019Review
- Complete Genome Sequence of the Wolbachia wAlbB Endosymbiont of Aedes albopictus.Genome biology and evolution · 2019Article
- Bacteria-Killing Type IV Secretion Systems.Frontiers in microbiology · 2019Review
- Interaction via the N terminus of the type IV secretion system (T4SS) protein VirB6 with VirB10 is required for VirB2 and VirB5 incorporation into T-pili and for T4SS function.The Journal of biological chemistry · 2018Article
- VirB8 homolog TraE from plasmid pKM101 forms a hexameric ring structure and interacts with the VirB6 homolog TraD.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Architecture of the type IV coupling protein complex of Legionella pneumophila.Nature microbiology · 2017Article
- Analyzing the role of CagV, a VirB8 homolog of the type IV secretion system ofFEBS open bio · 2017Article
- Use of chimeric type IV secretion systems to define contributions of outer membrane subassemblies for contact-dependent translocation.Molecular microbiology · 2017Article
3 more citing papers are in PubMed but not listed here.
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4 authors.
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Abstract
The Agrobacterium tumefaciens VirB/D4 type IV secretion system (T4SS) translocates DNA and protein substrates across the bacterial cell envelope. Six presumptive channel subunits of this T4SS (VirD4, VirBll, VirB6, VirB8, VirB2, and VirB9) form close contacts with the VirD2-T-strand transfer intermediate during export, as shown recently by a novel transfer DNA immunoprecipitation (TrIP) assay. Here, we characterize the contribution of the hydrophobic channel component VirB6 to substrate translocation. Results of reporter protein fusion and cysteine accessibility studies support a model for VirB6 as a polytopic membrane protein with a periplasmic N terminus, five transmembrane segments, and a cytoplasmic C terminus. TrIP studies aimed at characterizing the effects of VirB6 insertion and deletion mutations on substrate translocation identified several VirB6 functional domains: (i) a central region composed of a large periplasmic loop (P2) (residues 84 to 165) mediates the interaction of VirB6 with the exiting T-strand; (ii) a multi-membrane-spanning region carboxyl-terminal to loop P2 (residues 165 to 245) is required for substrate transfer from VirB6 to the bitopic membrane subunit VirB8; and (iii) the two terminal regions (residues 1 to 64 and 245 to 290) are required for substrate transfer to the periplasmic and outer membrane-associated VirB2 and VirB9 subunits. Our findings support a model whereby the periplasmic loop P2 comprises a portion of the secretion channel and distinct domains of VirB6 participate in channel subunit interactions required for substrate passage to the cell exterior.
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