Zaltsman, A., Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794, United States Lacroix, B., Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794, United States Gafni, Y., Institute of Plant Sciences, AgriculturalResearch Organization, Volcani Center, Bet Dagan 50250, Israel Citovsky, V., Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794, United States
One the most intriguing, yet least studied, aspects of the bacterium-host plant interaction is the role of the host ubiquitin/proteasome system (UPS) in the infection process. Increasing evidence indicates that pathogenic bacteria subvert the host UPS to facilitate infection. Although both mammalian and plant bacterial pathogens are known to use the host UPS, the first prokaryotic F-box protein, an essential component of UPS, was identified in Agrobacterium. During its infection, which culminates in genetic modification of the host cell, Agrobacterium transfers its T-DNA - as a complex (T-complex) with the bacterial VirE2 and host VIP1 proteins - into the host cell nucleus. There the T-DNA is uncoated from its protein components before undergoing integration into the host genome. It has been suggested that the host UPS mediates this uncoating process, but there is no evidence indicating that this activity can unmask the T-DNA molecule. Here we provide support for the idea that the plant UPS uncoats synthetic T-complexes via the Skp1/Cullin/F-box protein VBF pathway and exposes the T-DNA molecule to external enzymatic activity.
Disassembly of synthetic Agrobacterium T-DNA-protein complexes via the host SCFVBF ubiquitin-ligase complex pathway
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Zaltsman, A., Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794, United States Lacroix, B., Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794, United States Gafni, Y., Institute of Plant Sciences, AgriculturalResearch Organization, Volcani Center, Bet Dagan 50250, Israel Citovsky, V., Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794, United States
Disassembly of synthetic Agrobacterium T-DNA-protein complexes via the host SCFVBF ubiquitin-ligase complex pathway
One the most intriguing, yet least studied, aspects of the bacterium-host plant interaction is the role of the host ubiquitin/proteasome system (UPS) in the infection process. Increasing evidence indicates that pathogenic bacteria subvert the host UPS to facilitate infection. Although both mammalian and plant bacterial pathogens are known to use the host UPS, the first prokaryotic F-box protein, an essential component of UPS, was identified in Agrobacterium. During its infection, which culminates in genetic modification of the host cell, Agrobacterium transfers its T-DNA - as a complex (T-complex) with the bacterial VirE2 and host VIP1 proteins - into the host cell nucleus. There the T-DNA is uncoated from its protein components before undergoing integration into the host genome. It has been suggested that the host UPS mediates this uncoating process, but there is no evidence indicating that this activity can unmask the T-DNA molecule. Here we provide support for the idea that the plant UPS uncoats synthetic T-complexes via the Skp1/Cullin/F-box protein VBF pathway and exposes the T-DNA molecule to external enzymatic activity.