ArticleProceedings of the National Academy of Sciences of the United States of America2002
Detergent extraction identifies different VirB protein subassemblies of the type IV secretion machinery in the membranes of Agrobacterium tumefaciens.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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66 citing papers in PubMed.
- MtGRF8 interacts with MtSymCRK and prevents early bacteroid death during Medicago - Sinorhizobium symbiosis.The New phytologist · 2026Article
- Sneaky tactics: Ingenious immune evasion mechanisms ofVirulence · 2024Review
- Atypical rhizobia trigger nodulation and pathogenesis on the same legume hosts.Nature communications · 2024Article
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- Blue Native PAGE Analysis of Bacterial Secretion Complexes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Insight into the control of nodule immunity and senescence during Medicago truncatula symbiosis.Plant physiology · 2023Article
- DNA Methylation inmSystems · 2022Article
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- 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
- Isolation of a Membrane Protein Complex for Type VII Secretion in Staphylococcus aureus.Journal of bacteriology · 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
- Agrobacterium-mediated plant transformation: biology and applications.The arabidopsis book · 2017Article
- Multiple steps control immunity during the intracellular accommodation of rhizobia.Journal of experimental botany · 2015Article
- 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
- Article
- Cag type IV secretion system: CagI independent bacterial surface localization of CagA.PloS one · 2013Article
- Isolation of bacterial type IV machine subassemblies.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Alterations in Helicobacter pylori triggered by contact with gastric epithelial cells.Frontiers in cellular and infection microbiology · 2012Review
6 more citing papers are in PubMed but not listed here.
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Abstract
The VirB/D4 type IV secretion system of Agrobacterium tumefaciens translocates virulence factors (VirE2, VirF, and the VirD2-T-DNA complex) to plant cells. The membrane-bound translocation machinery consists of 12 proteins (VirB1-11 and VirD4) required for substrate translocation. Protein-protein interactions in the membranes were analyzed after extraction with the mild detergent dodecyl-beta-d-maltoside followed by separation under native conditions. Incubation of the membranes with increasing concentrations of the detergent differentially extracted virulence proteins. Separation of the solubilized proteins by blue native electrophoresis revealed cofractionation between two classes of protein complexes containing VirB7. The first class, consisting of major T-pilus component VirB2 and associated proteins VirB5 and VirB7, comigrated in the low molecular mass portion of the gel of about 100 kDa. The second class contains putative translocation complex core components VirB8, VirB9, and VirB10 in the high molecular mass portion of the gel larger than 232 kDa, as well as VirB7. Solubilized proteins were characterized further by gel filtration chromatography. This procedure separated T-pilus-associated proteins VirB2, VirB5, and VirB7 in the low molecular mass range from the other components of the translocation machinery and the substrates VirE2 and VirD2. Fractionation of VirB7-containing complexes (VirB7-VirB7 homodimers and VirB7-VirB9 heterodimers) suggested that they may link the T-pilus components to the core of the translocation machinery. Based on previously described VirB protein interactions and biochemical analysis of C58 wild type as well as of virB5 and virB6 deletion mutants, a model of T-pilus assembly in A. tumefaciens is suggested.
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