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The virA promoter is a host-range determinant in Agrobacterium tumefaciens (1993)

Turk, Stefan C. H. J. ; Nester, Eugene W. ; Hooykaas, Paul J. J.

Oxford, UK : Blackwell Publishing Ltd

Molecular microbiology 7 (1993), S. 0

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ISSN: 1365-2958

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology , Medicine

Notes: The limited host range (LHR) Agrobacterium tumefaciens strain Ag162 is an isolate with a narrow host range. Introduction of the wide host range (WHR) virA gene is essential for extending the host range to Kalanchoë daigremontiana. In this report we show that the region upstream of the ATG start codon is responsible for the LHR phenomenon and that this is probably due to the non-inducibility of the LHR virA promoter. By comparing the characteristics of the LHR and WHR VirA receptor proteins, it was found that the LHR VirA protein is able to activate the WHR VirG protein in the presence of acetosyringone and that this acetosyringone-dependent vir-induction is enhanced by the presence of d-glucose, as in the case of WHR VirA proteins. These results indicate that the domains, acting as receptors for sugars and phenolic signals, must be conserved between the LHR and WHR VirA receptor proteins.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb01162.x

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Localization of the VirA domain involved in acetosyringone-mediatedvir gene induction inAgrobacterium tumefaciens (1994)

Turk, Stefan C. H. J. ; Lange, Richard P. ; Regensburg-Tuïnk, Tonny J. G. ; [et al.]

Springer

Plant molecular biology 25 (1994), S. 899-907

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ISSN: 1573-5028

Keywords: Agrobacterium ; gene regulation ; sensor protein ; signal transduction ; VirA protein ; acetosyringone

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The VirA protein ofAgrobacterium 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 mediatedvir 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.