Agrobacterium rhizogenes GALLS Protein Contains Domains for ATP Binding, Nuclear Localization, and Type IV Secretion
| Autor: | Deborah M. Moyer, Annette C. Vergunst, Walt Ream, Amke den Dulk-Ras, Paul J. J. Hooykaas, Larry Hodges, Jason Neal-McKinney |
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| Rok vydání: | 2006 |
| Předmět: |
Agrobacterium
Molecular Sequence Data Mutant Virulence Plant Roots Microbiology DNA-binding protein Ion Channels Plant Microbiology Adenosine Triphosphate Bacterial Proteins Gall Secretion Amino Acid Sequence Molecular Biology Plant Diseases Cell Nucleus biology Binding protein Genetic Complementation Test Membrane Proteins Agrobacterium tumefaciens biology.organism_classification Protein Structure Tertiary DNA-Binding Proteins Biochemistry Sequence Alignment Rhizobium Signal Transduction |
| Zdroj: | Journal of Bacteriology, 188(23), 8222-8230 |
| ISSN: | 1098-5530 0021-9193 |
| Popis: | Agrobacterium tumefaciens and Agrobacterium rhizogenes are closely related plant pathogens that cause different diseases, crown gall and hairy root. Both diseases result from transfer, integration, and expression of plasmid-encoded bacterial genes located on the transferred DNA (T-DNA) in the plant genome. Bacterial virulence (Vir) proteins necessary for infection are also translocated into plant cells. Transfer of single-stranded DNA (ssDNA) and Vir proteins requires a type IV secretion system, a protein complex spanning the bacterial envelope. A. tumefaciens translocates the ssDNA-binding protein VirE2 into plant cells, where it binds single-stranded T-DNA and helps target it to the nucleus. Although some strains of A. rhizogenes lack VirE2, they are pathogenic and transfer T-DNA efficiently. Instead, these bacteria express the GALLS protein, which is essential for their virulence. The GALLS protein can complement an A. tumefaciens virE2 mutant for tumor formation, indicating that GALLS can substitute for VirE2. Unlike VirE2, GALLS contains ATP-binding and helicase motifs similar to those in TraA, a strand transferase involved in conjugation. Both GALLS and VirE2 contain nuclear localization sequences and a C-terminal type IV secretion signal. Here we show that mutations in any of these domains abolished the ability of GALLS to substitute for VirE2. |
| Databáze: | OpenAIRE |
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