ArticleProceedings of the National Academy of Sciences of the United States of America2008
Crystal structure of the Agrobacterium virulence complex VirE1-VirE2 reveals a flexible protein that can accommodate different partners.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 49 citations in OpenAlex.
- Myosin VIII and XI isoforms interact with the Agrobacterium VirE2 protein and facilitate its transport from the plasma membrane to the perinuclear region during plant transformation.Plant communications · 2026Article
- Cas9-mediated gene-editing frequency in microalgae is doubled by harnessing the interaction between importin α and phytopathogenic NLSs.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A tau class GST, OsGSTU5, interacts with VirE2 and modulates the Agrobacterium-mediated transformation in rice.Plant cell reports · 2022Article
- Incompatibility Group I1 (IncI1) Plasmids: Their Genetics, Biology, and Public Health Relevance.Microbiology and molecular biology reviews : MMBR · 2021Review
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- Insights into the transcriptomic response of the plant engineering bacterium Ensifer adhaerens OV14 during transformation.Scientific reports · 2019Article
- Biological and Structural Diversity of Type IV Secretion Systems.Microbiology spectrum · 2019Review
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- Chimeric Coupling Proteins Mediate Transfer of Heterologous Type IV Effectors through the Escherichia coli pKM101-Encoded Conjugation Machine.Journal of bacteriology · 2016Article
- Surface plasmon resonance imaging reveals multiple binding modes of Agrobacterium transformation mediator VirE2 to ssDNA.Nucleic acids research · 2015Article
- Mechanism and structure of the bacterial type IV secretion systems.Biochimica et biophysica acta · 2014Review
- Visualization of VirE2 protein translocation by the Agrobacterium type IV secretion system into host cells.MicrobiologyOpen · 2014Article
- Direct visualization of Agrobacterium-delivered VirE2 in recipient cells.The Plant journal : for cell and molecular biology · 2014Article
- Agrobacterium: nature's genetic engineer.Frontiers in plant science · 2014Article
- The roles of bacterial and host plant factors in Agrobacterium-mediated genetic transformation.The International journal of developmental biology · 2013Review
- The coupling protein Cagbeta and its interaction partner CagZ are required for type IV secretion of the Helicobacter pylori CagA protein.Infection and immunity · 2010Article
- 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
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Agrobacterium tumefaciens infects its plant hosts by a mechanism of horizontal gene transfer. This capability has led to its widespread use in artificial genetic transformation. In addition to DNA, the bacterium delivers an abundant ssDNA binding protein, VirE2, whose roles in the host include protection from cytoplasmic nucleases and adaptation for nuclear import. In Agrobacterium, VirE2 is bound to its acidic chaperone VirE1. When expressed in vitro in the absence of VirE1, VirE2 is prone to oligomerization and forms disordered filamentous aggregates. These filaments adopt an ordered solenoidal form in the presence of ssDNA, which was characterized previously by electron microscopy and three-dimensional image processing. VirE2 coexpressed in vitro with VirE1 forms a soluble heterodimer. VirE1 thus prevents VirE2 oligomerization and competes with its binding to ssDNA. We present here a crystal structure of VirE2 in complex with VirE1, showing that VirE2 is composed of two independent domains presenting a novel fold, joined by a flexible linker. Electrostatic interactions with VirE1 cement the two domains of VirE2 into a locked form. Comparison with the electron microscopy structure indicates that the VirE2 domains adopt different relative orientations. We suggest that the flexible linker between the domains enables VirE2 to accommodate its different binding partners.
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