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Herrera-Estrella, A. et al.

A bacterial peptide acting as a plant nuclear targeting signal: the amino-terminal portion of Agrobacterium VirD2 protein directs a beta-galactosidase fusion protein into tobacco nuclei.

Agrobacterium tumefaciens is a soil bacterium capable of transferring DNA to the genome of higher plants. Of the virulence region-encoded proteins of the tumor-inducing (Ti) plasmid of A. tumefaciens, the VirD1 and VirD2 proteins are essential for T-DNA transfer to plant cells. These two proteins have been shown to be directly responsible for the formation of T-strands. VirD2 was also shown to be firmly attached to the 5' termini of T-strands; these facts have led to its postulation as a pilot protein in the T-DNA transfer process and as a nucleus-targeting signal in plants. We have constructed a chimeric gene by fusing the virD2 gene and the Escherichia coli lacZ gene. Cell fractionation and electron microscopy studies with transgenic tobacco plants containing the VirD2-LacZ fusion protein indicate that the first 292 amino acids of VirD2 are able to direct the cytoplasmic protein beta-galactosidase to the plant nucleus. This provides an example of cross-kingdom nuclear localization between two free-living organisms: a bacterial peptide is capable of acting as a eukaryotic (plant) nuclear targeting signal.[1]

References

A bacterial peptide acting as a plant nuclear targeting signal: the amino-terminal portion of Agrobacterium VirD2 protein directs a beta-galactosidase fusion protein into tobacco nuclei. Herrera-Estrella, A., Van Montagu, M., Wang, K. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]

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