The VirE3 protein of Agrobacterium mimics a host cell function required for plant genetic transformation

The VirE3 protein of Agrobacterium mimics a host cell function required for plant genetic... To genetically transform plants, Agrobacterium exports its transferred DNA (T‐DNA) and several virulence (Vir) proteins into the host cell. Among these proteins, VirE3 is the only one whose biological function is completely unknown. Here, we demonstrate that VirE3 is transferred from Agrobacterium to the plant cell and then imported into its nucleus via the karyopherin α‐dependent pathway. In addition to binding plant karyopherin α, VirE3 interacts with VirE2, a major bacterial protein that directly associates with the T‐DNA and facilitates its nuclear import. The VirE2 nuclear import in turn is mediated by a plant protein, VIP1. Our data indicate that VirE3 can mimic this VIP1 function, acting as an ‘adapter’ molecule between VirE2 and karyopherin α and ‘piggy‐backing’ VirE2 into the host cell nucleus. As VIP1 is not an abundant protein, representing one of the limiting factors for transformation, Agrobacterium may have evolved to produce and export to the host cells its own virulence protein that at least partially complements the cellular VIP1 function necessary for the T‐DNA nuclear import and subsequent expression within the infected cell. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The EMBO Journal Wiley

The VirE3 protein of Agrobacterium mimics a host cell function required for plant genetic transformation

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Publisher
Wiley
Copyright
Copyright © 2013 Wiley Periodicals, Inc
ISSN
0261-4189
eISSN
1460-2075
D.O.I.
10.1038/sj.emboj.7600524
Publisher site
See Article on Publisher Site

Abstract

To genetically transform plants, Agrobacterium exports its transferred DNA (T‐DNA) and several virulence (Vir) proteins into the host cell. Among these proteins, VirE3 is the only one whose biological function is completely unknown. Here, we demonstrate that VirE3 is transferred from Agrobacterium to the plant cell and then imported into its nucleus via the karyopherin α‐dependent pathway. In addition to binding plant karyopherin α, VirE3 interacts with VirE2, a major bacterial protein that directly associates with the T‐DNA and facilitates its nuclear import. The VirE2 nuclear import in turn is mediated by a plant protein, VIP1. Our data indicate that VirE3 can mimic this VIP1 function, acting as an ‘adapter’ molecule between VirE2 and karyopherin α and ‘piggy‐backing’ VirE2 into the host cell nucleus. As VIP1 is not an abundant protein, representing one of the limiting factors for transformation, Agrobacterium may have evolved to produce and export to the host cells its own virulence protein that at least partially complements the cellular VIP1 function necessary for the T‐DNA nuclear import and subsequent expression within the infected cell.

Journal

The EMBO JournalWiley

Published: Jan 26, 2005

References

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