ArticleJournal of bacteriology1997
Interactions between VirB9 and VirB10 membrane proteins involved in movement of DNA from Agrobacterium tumefaciens into plant cells.
Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 95 citations in OpenAlex.
- DNA substrate-induced activation of the Agrobacterium VirB/VirD4 type IV secretion system.Journal of bacteriology · 2013Article
- Formation of complex extrachromosomal T-DNA structures in Agrobacterium tumefaciens-infected plants.Plant physiology · 2012Article
- 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
- An Agrobacterium VirB10 mutation conferring a type IV secretion system gating defect.Journal of bacteriology · 2011Article
- Phylogenomics reveals a diverse Rickettsiales type IV secretion system.Infection and immunity · 2010Review
- The structural biology of type IV secretion systems.Nature reviews. Microbiology · 2009Review
- Agrobacterium VirB10 domain requirements for type IV secretion and T pilus biogenesis.Molecular microbiology · 2009Article
- Article
- Immunogenicity of Anaplasma marginale type IV secretion system proteins in a protective outer membrane vaccine.Infection and immunity · 2007Article
- Detection of conjugation related type four secretion machinery in Aeromonas culicicola.PloS one · 2006Article
- The Brucella suis type IV secretion system assembles in the cell envelope of the heterologous host Agrobacterium tumefaciens and increases IncQ plasmid pLS1 recipient competence.Infection and immunity · 2006Article
- Agrobacterium tumefaciens oncogenic suppressors inhibit T-DNA and VirE2 protein substrate binding to the VirD4 coupling protein.Molecular microbiology · 2005Article
- Spatial location and requirements for the assembly of the Agrobacterium tumefaciens type IV secretion apparatus.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Agrobacterium tumefaciens VirB9, an outer-membrane-associated component of a type IV secretion system, regulates substrate selection and T-pilus biogenesis.Journal of bacteriology · 2005Article
- Structures of two core subunits of the bacterial type IV secretion system, VirB8 from Brucella suis and ComB10 from Helicobacter pylori.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Biogenesis, architecture, and function of bacterial type IV secretion systems.Annual review of microbiology · 2005Review
- Type IV secretion: the Agrobacterium VirB/D4 and related conjugation systems.Biochimica et biophysica acta · 2004Review
- Osa protein constitutes a strong oncogenic suppression system that can block vir-dependent transfer of IncQ plasmids between Agrobacterium cells and the establishment of IncQ plasmids in plant cells.Journal of bacteriology · 2004Article
- N-linked protein glycosylation is required for full competence in Campylobacter jejuni 81-176.Journal of bacteriology · 2004Article
- Agrobacterium tumefaciens VirB6 domains direct the ordered export of a DNA substrate through a type IV secretion System.Journal of molecular biology · 2004Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 11 VirB proteins from Agrobacterium tumefaciens are predicted to form a membrane-bound complex that mediates the movement of DNA from the bacterium into plant cells. The studies reported here on the possible VirB protein interactions in such a complex demonstrate that VirB9 and VirB10 can each form high-molecular-weight complexes after treatment with a chemical cross-linker. Analysis of nonpolar virB mutants showed that the formation of the VirB10 complexes does not occur in a virB9 mutant and that VirB9 and VirB10 are not components of the same cross-linked complex. VirB9, when stabilized by the concurrent expression of VirB7, was shown to be sufficient to permit VirB10 to cross-link into its usual high-molecular-weight forms in the absence of other Vir proteins. Randomly introduced single point mutations in virB9 resulted in Agrobacterium strains with severely attenuated virulence. Although some of the mutants contained wild-type levels of VirB9 and displayed an unaltered VirB9 cross-linking pattern, VirB10 cross-linking was drastically reduced. We conclude that specific amino acid residues in VirB9 are necessary for interaction with VirB10 resulting in the capacity of VirB10 to participate in high-molecular-weight complexes that can be visualized by chemical cross-linking.
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