Localization of the VirA domain involved in acetosyringone-mediated vir gene induction in Agrobacterium tumefaciens

The VirA protein of Agrobacterium tumefaciens is thought to be a receptor for plant phenolic compounds such as acetosyringone. Although it is not known whether the interaction between VirA and the phenolics is direct or requires other phenolic-binding proteins, it is shown in this study that the fir...

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Bibliographic Details
Published in:	Plant molecular biology Vol. 25; no. 5; pp. 899 - 907
Main Authors:	Turk, S.C.H.J. (Leiden Univ. (Netherlands). Inst. of Molecular Plant Sciences), Lange, R.P. van, Regensburg-Tuink, T.J.G, Hooykaas, P.J.J
Format:	Journal Article
Language:	English
Published:	Netherlands 01-08-1994
Subjects:	Acetophenones - pharmacology AGROBACTERIUM TUMEFACIENS Agrobacterium tumefaciens - genetics Agrobacterium tumefaciens - pathogenicity Amino Acid Sequence Bacterial Proteins - biosynthesis Bacterial Proteins - genetics Base Sequence Chemoreceptor Cells COMPOSE PHENOLIQUE COMPUESTOS FENOLICOS DNA Mutational Analysis Escherichia coli Proteins GENE Gene Expression Regulation, Bacterial - drug effects GENES Genes, Bacterial Membrane Proteins - biosynthesis Membrane Proteins - genetics Molecular Sequence Data PHENOLIC COMPOUNDS Receptors, Cell Surface Recombinant Fusion Proteins - biosynthesis Sequence Deletion Sequence Homology, Amino Acid Signal Transduction - genetics Structure-Activity Relationship Transcriptional Activation Virulence - genetics Virulence Factors
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Summary:	The VirA protein of Agrobacterium tumefaciens is thought to be a receptor for plant phenolic compounds such as acetosyringone. Although it is not known whether the interaction between VirA and the phenolics is direct or requires other phenolic-binding proteins, it is shown in this study that the first 280 amino acids of the VirA protein are not essential for the acetosyringone mediated vir gene induction response. Considering the fact that the cytoplasmic region between the amino acids 283 and 304 is highly conserved between the different VirA proteins, and that deletion of this region abolishes VirA activity, we suggest that the acetosyringone receptor domain is located in this cytoplasmic domain of the VirA protein.
Bibliography:	F30 9500723 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0167-4412 1573-5028
DOI:	10.1007/BF00028884