ArticleJournal of bacteriology1997
VirB1, a component of the T-complex transfer machinery of Agrobacterium tumefaciens, is processed to a C-terminal secreted product, VirB1.
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 48 papers.
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Who cites it
48 citing papers in PubMed.
- Conjugation's Toolkit: the Roles of Nonstructural Proteins in Bacterial Sex.Journal of bacteriology · 2023Review
- Glycoside Hydrolase Genes Are Required for Virulence of Agrobacterium tumefaciens onApplied and environmental microbiology · 2019Article
- Insights into the transcriptomic response of the plant engineering bacterium Ensifer adhaerens OV14 during transformation.Scientific reports · 2019Article
- GROWTH POLE RING protein forms a 200-nm-diameter ring structure essential for polar growth and rod shape inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Bacteria-Killing Type IV Secretion Systems.Frontiers in microbiology · 2019Review
- Agrobacterium-mediated plant transformation: biology and applications.The arabidopsis book · 2017Article
- Complete sequence and detailed analysis of the first indigenous plasmid from Xanthomonas oryzae pv. oryzicola.BMC microbiology · 2015Article
- The bifunctional cell wall hydrolase CwlT is needed for conjugation of the integrative and conjugative element ICEBs1 in Bacillus subtilis and B. anthracis.Journal of bacteriology · 2014Article
- A functional peptidoglycan hydrolase characterized from T4SS in 89K pathogenicity island of epidemic Streptococcus suis serotype 2.BMC microbiology · 2014Article
- Bacterial Type IV secretion systems: versatile virulence machines.Future microbiology · 2012Review
- Article
- Type IV secretion systems: versatility and diversity in function.Cellular microbiology · 2010Review
- Phylogenomics reveals a diverse Rickettsiales type IV secretion system.Infection and immunity · 2010Review
- Agrobacterium type IV secretion system and its substrates form helical arrays around the circumference of virulence-induced cells.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The structural biology of type IV secretion systems.Nature reviews. Microbiology · 2009Review
- Article
- Four VirB6 paralogs and VirB9 are expressed and interact in Ehrlichia chaffeensis-containing vacuoles.Journal of bacteriology · 2009Article
- Secretome analysis uncovers an Hcp-family protein secreted via a type VI secretion system in Agrobacterium tumefaciens.Journal of bacteriology · 2008Article
- The type IV secretion system component VirB5 binds to the trans-zeatin biosynthetic enzyme Tzs and enables its translocation to the cell surface of Agrobacterium tumefaciens.Journal of bacteriology · 2008Article
- Pseudomonas syringae lytic transglycosylases coregulated with the type III secretion system contribute to the translocation of effector proteins into plant cells.Journal of bacteriology · 2007Article
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4 authors.
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Abstract
During genetic transformation of plant cells by Agrobacterium tumefaciens, 11 VirB proteins and VirD4 are proposed to form a transmembrane bridge to transfer a DNA-protein complex (T-complex) into the plant cytoplasm. In this study, the localization of the first product of the virB operon, VirB1, was studied in detail. While full-length VirB1 localized mostly to the inner membrane, an immunoreactive VirB1 product was found as soluble processed form, designated VirB1*. Equal amounts of VirB1* could be detected in concentrated culture supernatants versus associated with the cell. VirB1* was purified from the supernatant of vir-induced cells by ammonium sulfate precipitation and Q-Sepharose chromatography. Sequence analysis of the N terminus of VirB1* localized the processing site after amino acid 172 of VirB1. Cell-associated VirB1* was partly removed by vortexing, suggesting a loose association with the cell or active secretion. However, cross-linking and coimmunoprecipitation showed a close association of cell-bound VirB1* with the VirB9-VirB7 heterodimer, a membrane-associated component of the T-complex transfer machinery. Homologies of the N-terminal part of VirB1 to bacterial transglycosylases suggest that it may assist T-complex transfer by local lysis of the bacterial cell wall, whereas the exposed localization of the C-terminal processing product VirB1* predicts direct interaction with the plant. Thus, VirB1 may be a bifunctional protein where both parts have different functions in T-complex transfer from Agrobacterium to plant cells.
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