ArticleJournal of bacteriology2000
The Agrobacterium T-DNA transport pore proteins VirB8, VirB9, and VirB10 interact with one another.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
63 citing papers in PubMed, 122 citations in OpenAlex.
- Lifestyle-associated variation in type IV secretion systems between phytopathogenic and environmentalMicrobial genomics · 2026Article
- Protein-Protein Interactions: Yeast Two Hybrid.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Protein interactions within and between two F-type type IV secretion systems.Molecular microbiology · 2020Article
- Identification and evaluation of UL36 protein from Dermacentor silvarum salivary gland and its interaction with Anaplasma ovis VirB10.Parasites & vectors · 2020Article
- 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
- Use of chimeric type IV secretion systems to define contributions of outer membrane subassemblies for contact-dependent translocation.Molecular microbiology · 2017Article
- Analyzing the role of CagV, a VirB8 homolog of the type IV secretion system ofFEBS open bio · 2017Article
- Super-Resolution Imaging of Protein Secretion Systems and the Cell Surface of Gram-Negative Bacteria.Frontiers in cellular and infection microbiology · 2017Review
- Structural Analysis and Inhibition of TraE from the pKM101 Type IV Secretion System.The Journal of biological chemistry · 2016Article
- VirB8-like protein TraH is crucial for DNA transfer in Enterococcus faecalis.Scientific reports · 2016Article
- Article
- TraK and TraB are conserved outer membrane proteins of the Neisseria gonorrhoeae Type IV secretion system and are expressed at low levels in wild-type cells.Journal of bacteriology · 2014Article
- Association and evidence for linked recognition of type IV secretion system proteins VirB9-1, VirB9-2, and VirB10 in Anaplasma marginale.Infection and immunity · 2012Article
- The dimer interface of Agrobacterium tumefaciens VirB8 is important for type IV secretion system function, stability, and association of VirB2 with the core complex.Journal of bacteriology · 2011Article
- An in vivo high-throughput screening approach targeting the type IV secretion system component VirB8 identified inhibitors of Brucella abortus 2308 proliferation.Infection and immunity · 2011Article
- Article
- Agrobacterium tumefaciens type IV secretion protein VirB3 is an inner membrane protein and requires VirB4, VirB7, and VirB8 for stabilization.Journal of bacteriology · 2010Article
- The structural biology of type IV secretion systems.Nature reviews. Microbiology · 2009Review
- Interactions between Brucella suis VirB8 and its homolog TraJ from the plasmid pSB102 underline the dynamic nature of type IV secretion systems.Journal of bacteriology · 2009Article
- Agrobacterium VirB10 domain requirements for type IV secretion and T pilus biogenesis.Molecular microbiology · 2009Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The VirB proteins of Agrobacterium tumefaciens form a transport pore to transfer DNA from bacteria to plants. The assembly of the transport pore will require interaction among the constituent proteins. The identification of proteins that interact with one another can provide clues to the assembly of the transport pore. We studied interaction among four putative transport pore proteins, VirB7, VirB8, VirB9 and VirB10. Using the yeast two-hybrid assay, we observed that VirB8, VirB9, and VirB10 interact with one another. In vitro studies using protein fusions demonstrated that VirB10 interacts with VirB9 and itself. These results suggest that the outer membrane VirB7-VirB9 complex interacts with the inner membrane proteins VirB8 and VirB10 for the assembly of the transport pore. Fusions that contain small, defined segments of the proteins were used to define the interaction domains of VirB8 and VirB9. All interaction domains of both proteins mapped to the N-terminal half of the proteins. Two separate domains at the N- and C-terminal ends of VirB9 are involved in its homotypic interaction, suggesting that VirB9 forms a higher oligomer. We observed that the alteration of serine at position 87 of VirB8 to leucine abolished its DNA transfer function. Studies on the interaction of the mutant protein with the other VirB proteins showed that the VirB8S87L mutant is defective in interaction with VirB9. The mutant, however, interacted efficiently with VirB8 and VirB10, suggesting that the VirB8-VirB9 interaction is essential for DNA transfer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.