ArticleJournal of bacteriology2010
Agrobacterium tumefaciens type IV secretion protein VirB3 is an inner membrane protein and requires VirB4, VirB7, and VirB8 for stabilization.
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 35 papers.
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Who cites it
35 citing papers in PubMed, 60 citations in OpenAlex.
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- The R plasmid pRAS2 in the fish pathogenFrontiers in microbiology · 2026Article
- Type IV secretion systems: from structures to mechanisms.The EMBO journal · 2025Review
- The assembly of a hybrid type IV secretion system by a Crohn's disease-associated Escherichia coli strain.Nature communications · 2025Article
- The type IV secretion system ofMicrobial genomics · 2025Article
- Metagenomic insights into the response of soil microbial communities to pathogenicFrontiers in plant science · 2024Article
- Phyllosphere bacterial community dynamics in response to bacterial wildfire disease: succession and interaction patterns.Frontiers in plant science · 2024Article
- Characterization of ConE, the VirB4 Homolog of the Integrative and Conjugative Element ICEJournal of bacteriology · 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
- Antibacterial contact-dependent proteins secreted by Gram-negative cystic fibrosis respiratory pathogens.Trends in microbiology · 2022Review
- Article
- Genetic Profiling ofPathogens (Basel, Switzerland) · 2019Article
- Structure of a VirD4 coupling protein bound to a VirB type IV secretion machinery.The EMBO journal · 2017Article
- Analyzing the role of CagV, a VirB8 homolog of the type IV secretion system ofFEBS open bio · 2017Article
- VirB8-like protein TraH is crucial for DNA transfer in Enterococcus faecalis.Scientific reports · 2016Article
- Article
- Two novel membrane proteins, TcpD and TcpE, are essential for conjugative transfer of pCW3 in Clostridium perfringens.Journal of bacteriology · 2015Article
- Article
- Pan-genome analysis of human gastric pathogen H. pylori: comparative genomics and pathogenomics approaches to identify regions associated with pathogenicity and prediction of potential core therapeutic targets.BioMed research international · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Agrobacterium tumefaciens VirB proteins assemble a type IV secretion apparatus and a T-pilus for secretion of DNA and proteins into plant cells. The pilin-like protein VirB3, a membrane protein of unknown topology, is required for the assembly of the T-pilus and for T-DNA secretion. Using PhoA and green fluorescent protein (GFP) as periplasmic and cytoplasmic reporters, respectively, we demonstrate that VirB3 contains two membrane-spanning domains and that both the N and C termini of the protein reside in the cytoplasm. Fusion proteins with GFP at the N or C terminus of VirB3 were fluorescent and, like VirB3, localized to a cell pole. Biochemical fractionation studies demonstrated that VirB3 proteins encoded by three Ti plasmids, the octopine Ti plasmid pTiA6NC, the supervirulent plasmid pTiBo542, and the nopaline Ti plasmid pTiC58, are inner membrane proteins and that VirB4 has no effect on membrane localization of pTiA6NC-encoded VirB3 (pTiA6NC VirB3). The pTiA6NC and pTiBo542 VirB2 pilins, like VirB3, localized to the inner membrane. The pTiC58 VirB4 protein was earlier found to be essential for stabilization of VirB3. Stabilization of pTiA6NC VirB3 requires not only VirB4 but also two additional VirB proteins, VirB7 and VirB8. A binary interaction between VirB3 and VirB4/VirB7/VirB8 is not sufficient for VirB3 stabilization. We hypothesize that bacteria use selective proteolysis as a mechanism to prevent assembly of unproductive precursor complexes under conditions that do not favor assembly of large macromolecular structures.
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