V. Shingler et T. Moore, SENSING OF AROMATIC-COMPOUNDS BY THE DMPR TRANSCRIPTIONAL ACTIVATOR OF PHENOL-CATABOLIZING PSEUDOMONAS SP STRAIN CF600, Journal of bacteriology, 176(6), 1994, pp. 1555-1560
The dmp operon of the pVI150 catabolic plasmid of Pseudomonas sp. stra
in CF600 encodes the enzymes involved in the catabolism of phenol and
methylphenols. The regulator of this dmp pathway, DmpR, is a member of
the NtrC family of transcriptional activators and controls transcript
ion of the dmp operon in response to aromatic effector compounds (V. S
hingler, M. Bartilson, and T. Moore, J. Bacteriol. 175:1596-1604, 1993
). Using a lux gene fusion reporter system, in which the DmpR-regulate
d operon promoter controls the expression of luciferase activity, we h
ave shown in the study reported here that DmpR is activated by, but re
sponds differentially to, the presence of a wide range of aromatic com
pounds. In many microbial regulatory systems, including some members o
f the NtrC family, the response to environmental fluctuations involves
information transfer from surface sensory proteins to transcriptional
regulators. However, DmpR-mediated activation of phenol metabolism in
response to aromatic compounds occurs in the absence of a specific se
nsory protein. We used hybrids between DmpR and XylR, a structurally r
elated regulator of toluene and xylene metabolism, to demonstrate that
it is the amino-terminal domains of these regulators that determine t
he specificity of transcriptional activation. The results suggest that
it is the direct interaction of aromatic compounds with the DmpR and
XylR proteins that regulates their transcriptional promoting activity.