ArticleJournal of bacteriology2000
The N- and C-terminal portions of the Agrobacterium VirB1 protein independently enhance tumorigenesis.
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 26 papers.
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Who cites it
26 citing papers in PubMed, 50 citations in OpenAlex.
- Type IV secretion systems: reconciling diversity through a unified nomenclature.FEMS microbiology reviews · 2026Review
- Article
- Antibacterial contact-dependent proteins secreted by Gram-negative cystic fibrosis respiratory pathogens.Trends in microbiology · 2022Review
- Bacteria-Killing Type IV Secretion Systems.Frontiers in microbiology · 2019Review
- Lytic transglycosylases: concinnity in concision of the bacterial cell wall.Critical reviews in biochemistry and molecular biology · 2017Review
- Agrobacterium-mediated plant transformation: biology and applications.The arabidopsis book · 2017Article
- Review
- 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
- Biological diversity of prokaryotic type IV secretion systems.Microbiology and molecular biology reviews : MMBR · 2009Review
- Article
- 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
- VirB1* promotes T-pilus formation in the vir-Type IV secretion system of Agrobacterium tumefaciens.Journal of bacteriology · 2007Article
- Predicted hexameric structure of the Agrobacterium VirB4 C terminus suggests VirB4 acts as a docking site during type IV secretion.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Type IV secretion: the Agrobacterium VirB/D4 and related conjugation systems.Biochimica et biophysica acta · 2004Review
- VirB1 orthologs from Brucella suis and pKM101 complement defects of the lytic transglycosylase required for efficient type IV secretion from Agrobacterium tumefaciens.Journal of bacteriology · 2004Article
- Conjugative plasmid transfer in gram-positive bacteria.Microbiology and molecular biology reviews : MMBR · 2003Review
- Peptide linkage mapping of the Agrobacterium tumefaciens vir-encoded type IV secretion system reveals protein subassemblies.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
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
Genetic transformation of plants by Agrobacterium tumefaciens is mediated by a virulence (vir)-specific type IV secretion apparatus assembled from 11 VirB proteins and VirD4. VirB1, targeted to the periplasm by an N-terminal signal peptide, is processed to yield VirB1*, comprising the C-terminal 73 amino acids. The N-terminal segment, which shares homology with chicken egg white lysozyme as well as lytic transglycosylases, may provide local lysis of the peptidoglycan cell wall to create channels for transporter assembly. Synthesis of VirB1* followed by its secretion to the exterior of the cell suggests that VirB1* may also have a role in virulence. In the present study, we provide evidence for the dual roles of VirB1 in tumorigenesis as well as the requirements for processing and secretion of VirB1*. Complementation of a virB1 deletion strain with constructs expressing either the N-terminal lysozyme-homologous region or VirB1* results in tumors intermediate in size between those induced by a wild-type strain and a virB1 deletion strain, suggesting that each domain has a unique role in tumorigenesis. The secretion of VirB1* translationally fused to the signal peptide indicates that processing and secretion are not coupled. When expressed independently of all other vir genes, VirB1 was processed and VirB1* was secreted. When restricted to the cytoplasm by deletion of the signal peptide, VirB1 was neither processed nor secreted and did not restore virulence to the virB1 deletion strain. Thus, factors that mediate processing of VirB1 and secretion of VirB1* are localized in the periplasm or outer membrane and are not subject to vir regulation.
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