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Journal of Bacteriology, January 2009, p. 355-364, Vol. 191, No. 1
0021-9193/09/$08.00+0     doi:10.1128/JB.01018-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The Agrobacterium rhizogenes GALLS Gene Encodes Two Secreted Proteins Required for Genetic Transformation of Plants{triangledown}

Larry D. Hodges,1 Lan-Ying Lee,2 Henry McNett,1 Stanton B. Gelvin,2 and Walt Ream1*

Department of Microbiology, Oregon State University, Corvallis, Oregon 97331,1 Department of Biological Sciences, Purdue University, West Lafayette, Indiana 479072

Received 23 July 2008/ Accepted 20 October 2008

Agrobacterium tumefaciens and Agrobacterium rhizogenes are related pathogens that cause crown gall and hairy root diseases, which result from integration and expression of bacterial genes in the plant genome. Single-stranded DNA (T strands) and virulence proteins are translocated into plant cells by a type IV secretion system. VirD2 nicks a specific DNA sequence, attaches to the 5' end, and pilots the DNA into plant cells. A. tumefaciens translocates single-stranded DNA-binding protein VirE2 into plant cells where it likely binds T strands and may aid in targeting them into the nucleus. Although some A. rhizogenes strains lack VirE2, they transfer T strands efficiently due to the GALLS gene, which complements an A. tumefaciens virE2 mutant for tumor formation. Unlike VirE2, full-length GALLS (GALLS-FL) contains ATP-binding and helicase motifs similar to those in TraA, a strand transferase involved in conjugation. GALLS-FL and VirE2 contain nuclear localization signals (NLS) and secretion signals. Mutations in any of these domains abolish the ability of the GALLS gene to substitute for virE2. Here, we show that the GALLS gene encodes two proteins from one open reading frame: GALLS-FL and a protein comprised of the C-terminal domain, which initiates at an internal in-frame start codon. On some hosts, both GALLS proteins were required to substitute for VirE2. GALLS-FL tagged with yellow fluorescent protein localized to the nucleus of tobacco cells in an NLS-dependent manner. In plant cells, the GALLS proteins interacted with themselves, VirD2, and each other. VirD2 interacted with GALLS-FL and localized inside the nucleus, where its predicted helicase activity may pull T strands into the nucleus.

* Corresponding author. Mailing address: Department of Microbiology, Oregon State University, Corvallis, OR 97331. Phone: (541) 737-1791. Fax: (541) 737-0496. E-mail: reamw{at}orst.edu

{triangledown} Published ahead of print on 24 October 2008.

Journal of Bacteriology, January 2009, p. 355-364, Vol. 191, No. 1
0021-9193/09/$08.00+0     doi:10.1128/JB.01018-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gelvin, S. B. (2009). Agrobacterium in the Genomics Age. Plant Physiol. 150: 1665-1676 [Full Text]  


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