Please use this identifier to cite or link to this item: https://doi.org/10.3389/fpls.2020.00464
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dc.titleAgrobacterium VirE3 Uses Its Two Tandem Domains at the C-Terminus to Retain Its Companion VirE2 on the Cytoplasmic Side of the Host Plasma Membrane
dc.contributor.authorLi, X.
dc.contributor.authorZhu, T.
dc.contributor.authorTu, H.
dc.contributor.authorPan, S.Q.
dc.date.accessioned2021-08-24T02:35:04Z
dc.date.available2021-08-24T02:35:04Z
dc.date.issued2020
dc.identifier.citationLi, X., Zhu, T., Tu, H., Pan, S.Q. (2020). Agrobacterium VirE3 Uses Its Two Tandem Domains at the C-Terminus to Retain Its Companion VirE2 on the Cytoplasmic Side of the Host Plasma Membrane. Frontiers in Plant Science 11 : 464. ScholarBank@NUS Repository. https://doi.org/10.3389/fpls.2020.00464
dc.identifier.issn1664-462X
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/198915
dc.description.abstractAgrobacterium tumefaciens is the causal agent of crown gall disease in nature; in the laboratory the bacterium is widely used for plant genetic modification. The bacterium delivers a single-stranded transferred DNA (T-DNA) and a group of crucial virulence proteins into host cells. A putative T-complex is formed inside host cells that is composed of T-DNA and virulence proteins VirD2 and VirE2, which protect the foreign DNA from degradation and guide its way into the host nucleus. However, little is known about how the T-complex is assembled inside host cells. We combined the split-GFP and split-sfCherry labeling systems to study the interaction of Agrobacterium-delivered VirE2 and VirE3 in host cells. Our results indicated that VirE2 co-localized with VirE3 on the cytoplasmic side of the host cellular membrane upon the delivery. We identified and characterized two tandem domains at the VirE3 C-terminus that interacted with VirE2 in vitro. Deletion of these two domains abolished the VirE2 accumulation on the host plasma membrane and affected the transformation. Furthermore, the two VirE2-interacting domains of VirE3 exhibited different affinities with VirE2. Collectively, this study demonstrates that the anchorage protein VirE3 uses the two tandem VirE2-interacting domains to facilitate VirE2 protection for T-DNA at the cytoplasmic side of the host cell entrance. @ Copyright @ 2020 Li, Zhu, Tu and Pan.
dc.publisherFrontiers Media S.A.
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.sourceScopus OA2020
dc.subjectAgrobacterium
dc.subjectplasma membrane
dc.subjectT-complex
dc.subjectT-DNA
dc.subjectVirE2
dc.subjectVirE3
dc.typeArticle
dc.contributor.departmentDEPT OF BIOLOGICAL SCIENCES
dc.contributor.departmentDEPT OF BIOCHEMISTRY
dc.description.doi10.3389/fpls.2020.00464
dc.description.sourcetitleFrontiers in Plant Science
dc.description.volume11
dc.description.page464
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