ArticleNucleic acids research2003
Analysis of Vir protein translocation from Agrobacterium tumefaciens using Saccharomyces cerevisiae as a model: evidence for transport of a novel effector protein VirE3.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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54 citing papers in PubMed, 122 citations in OpenAlex.
- A bacterial-killing type IV secretion system as a hidden antifungal device.Science advances · 2026Article
- Cellulose Degradation Enzymes in Filamentous Fungi, A Bioprocessing Approach Towards Biorefinery.Molecular biotechnology · 2025Review
- T4SEpp: A pipeline integrating protein language models to predict bacterial type IV secreted effectors.Computational and structural biotechnology journal · 2024Article
- Article
- Opportunistic Bacteria of Grapevine Crown Galls Are Equipped with the Genomic Repertoire for Opine Utilization.Genome biology and evolution · 2023Article
- Soil bacterium manipulates antifungal weapons by sensing intracellular type IVA secretion system effectors of a competitor.The ISME journal · 2023Article
- Recruitment of heterologous substrates by bacterial secretion systems for transkingdom translocation.Frontiers in cellular and infection microbiology · 2023Review
- A tau class GST, OsGSTU5, interacts with VirE2 and modulates the Agrobacterium-mediated transformation in rice.Plant cell reports · 2022Article
- JAZ8 Interacts With VirE3 Attenuating Agrobacterium Mediated Root Tumorigenesis.Frontiers in plant science · 2021Article
- Article
- CRISPR/Cas9 Mutagenesis by Translocation of Cas9 Protein Into Plant Cells via theFrontiers in genome editing · 2020Article
- Overexpression of VIRE2-INTERACTING PROTEIN2 in Arabidopsis regulates genes involved in Agrobacterium-mediated plant transformation and abiotic stresses.Scientific reports · 2019Article
- Natural and Artificial Strategies To Control the Conjugative Transmission of Plasmids.Microbiology spectrum · 2018Review
- Effective prediction of bacterial type IV secreted effectors by combined features of both C-termini and N-termini.Journal of computer-aided molecular design · 2017Article
- Architecture of the type IV coupling protein complex of Legionella pneumophila.Nature microbiology · 2017Article
- Article
- Article
- Agrobacterium-mediated plant transformation: biology and applications.The arabidopsis book · 2017Article
- Chimeric Coupling Proteins Mediate Transfer of Heterologous Type IV Effectors through the Escherichia coli pKM101-Encoded Conjugation Machine.Journal of bacteriology · 2016Article
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Agrobacterium tumefaciens causes crown gall disease on a variety of plants. During the infection process Agrobacterium transfers a nucleoprotein complex, the VirD2 T-complex, and at least two Vir proteins, VirE2 and VirF, into the plant cell via the VirB/VirD4 type IV secretion system. Recently, we found that T-DNA could also be transferred from Agrobacterium to Saccharomyces cerevisiae. Here, we describe a novel method to also detect trans-kingdom Vir protein transfer from Agrobacterium to yeast, using the Cre/lox system. Protein fusions between Cre and VirE2 or VirF were expressed in AGROBACTERIUM: Transfer of the Cre-Vir fusion proteins from Agrobacterium to yeast was monitored by a selectable excision event resulting from site-specific recombination mediated by Cre on a lox-flanked transgene in yeast. The VirE2 and VirF proteins were transported to yeast via the virB-encoded transfer system in the presence of coupling factor VirD4, analogous to translocation into plant cells. The yeast system therefore provides a suitable and fast model system to study basic aspects of trans-kingdom protein transport from Agrobacterium into host cells. Using this method we showed that VirE2 and VirF protein transfer was inhibited by the presence of the Osa protein. Besides, we found evidence for a novel third effector protein, VirE3, which has a similar C-terminal signature to VirE2 and VirF.
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