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Journal of Bacteriology, November 1998, p. 5632-5638, Vol. 180, No. 21
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
The Phenolic Recognition Profiles of the Agrobacterium
tumefaciens VirA Protein Are Broadened by a High Level of the
Sugar Binding Protein ChvE
Wen-Tao
Peng,
Yong-Woog
Lee,
and
Eugene W.
Nester*
Department of Microbiology, University of
Washington, Seattle, Washington 98195
Received 29 June 1998/Accepted 1 September 1998
The formation of crown gall tumors by Agrobacterium
tumefaciens requires that the virulence (vir) genes
be induced by chemical signals which consist of specific phenolic
compounds and monosaccharides, synthesized at plant wound sites. Signal
transduction in the activation of these genes is mediated by the
VirA-VirG two-component regulatory system, together with ChvE, a
glucose-galactose binding protein which interacts with VirA. We have
previously presented genetic evidence that virA senses
phenolic compounds directly (Y.-W. Lee, S. Jin, W.-S. Sim, and E. W. Nester, Proc. Natl. Acad. Sci. USA 92:12245-12249,
1995). The vir genes of strain KU12 can be induced by
4-hydroxyacetophenone, p-coumaric acid, and phenol, whereas these same phenolic compounds are weak inducers of the vir
genes of strain A6. In this report, we show that a specific inducing sugar can broaden the specificity of the phenolic compound which VirA
senses. 4-Hydroxyacetophenone and other related phenolic compounds
function as inducing phenolic compounds with the virA gene
of A6 if arabinose replaces glucose as the inducing sugar. We further
demonstrate that this broadened specificity for phenolic inducers
results from the increased level of ChvE through induction by arabinose
via the regulatory protein GbpR. If high levels of ChvE are present,
then poorly inducing phenolic compounds can induce the vir
genes to high levels in combination with glucose. Comparing the
induction response of the wild type and that of a VirA mutant with a
mutation in its receiver domain revealed that the activity of the
receiver domain is controlled by the periplasmic domain. We
discuss these observations in terms of how VirA senses and transduces
signals elicited by the two classes of plant signal molecules.
*
Corresponding author. Mailing address: Department of
Microbiology, Box 357242, University of Washington, Seattle, WA
98195. Phone: (206) 616-8588. Fax: (206) 543-8297. E-mail:
gnester{at}u.washington.edu.

Present address: Department of Legal Medicine, College of Medicine,
Korea University, 126-1, 5-ga, Anam-dong, Sungbuk-gu,
Seoul,
136-701, Korea.
Journal of Bacteriology, November 1998, p. 5632-5638, Vol. 180, No. 21
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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