Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein
| Autor: | Chia-Hwa Chang, Stephen C. Winans |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Virulence Factors
DNA Mutational Analysis Molecular Sequence Data Microbiology DNA-binding protein Bacterial Proteins VirA protein Molecular Biology Alleles Aspartic Acid Base Sequence Virulence biology Membrane Transport Proteins Agrobacterium tumefaciens Periplasmic space Plants biology.organism_classification Protein Structure Tertiary DNA-Binding Proteins Regulon Biochemistry Mutagenesis Periplasmic Binding Proteins biology.protein bacteria Phosphorylation Linker Signal Transduction Transcription Factors Research Article |
| Zdroj: | Journal of Bacteriology. 174:7033-7039 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.174.21.7033-7039.1992 |
| Popis: | VirA and VirG activate the Agrobacterium tumefaciens vir regulon in response to phenolic compounds, monosaccharides, and acidity released from plant wound sites. VirA contains an amino-terminal periplasmic domain and three cytoplasmic domains: a linker, a protein kinase, and a phosphoryl receiver. We constructed internal deletions of virA that truncate one or more domains and tested the ability of the resulting proteins to mediate environmentally responsive vir gene activation in vivo. The periplasmic domain is required for sensing of monosaccharides (in agreement with earlier results), while the linker domain is required for sensing of phenolic compounds and acidity. The phosphoryl receiver domain of VirA plays an inhibitory role in signal transduction that may be modulated by phosphorylation. The carboxy terminus of the protein was also dispensable for tumorigenesis, while the periplasmic domain was required. |
| Databáze: | OpenAIRE |
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