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

Proc Natl Acad Sci U S A. 1990 Dec;87(24):9534-7. doi: 10.1073/pnas.87.24.9534.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics*
  • Cell Nucleus / metabolism
  • Kinetics
  • Microscopy, Electron
  • Nicotiana / genetics
  • Nicotiana / metabolism*
  • Plants, Toxic*
  • Recombinant Fusion Proteins / metabolism
  • Recombinant Fusion Proteins / ultrastructure
  • Rhizobium / genetics*
  • Rhizobium / metabolism
  • Virulence Factors*
  • beta-Galactosidase / genetics*
  • beta-Galactosidase / metabolism
  • beta-Galactosidase / ultrastructure

Substances

  • Bacterial Proteins
  • Recombinant Fusion Proteins
  • Virulence Factors
  • beta-Galactosidase