Journal of Bacteriology, January 2000, p. 405-417, Vol. 182, No. 2
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Swiss Federal Institute for Environmental Science and Technology and Swiss Federal Institute of Technology, CH-8600 Dübendorf,1 and Institute of Biotechnology, Swiss Federal Institute of Technology, CH-8093 Zürich,2 Switzerland
Received 26 April 1999/Accepted 11 October 1999
The regulation of 2-hydroxybiphenyl and 2,2'-dihydroxybiphenyl
degradation in Pseudomonas azelaica is mediated by the
regulatory gene, hbpR. The hbpR gene encodes a
63-kDa protein belonging to the NtrC family of prokaryotic
transcriptional activators and having the highest homology to members
of the XylR/DmpR subclass. Disruption of the hbpR
gene in P. azelaica and complementation in
trans showed that the HbpR protein was the key
regulator for 2-hydroxybiphenyl metabolism. Induction experiments with
P. azelaica and Escherichia coli containing
luxAB-based transcriptional fusions revealed that HbpR
activates transcription from a promoter
(PhbpC) in front of the first gene for
2-hydroxybiphenyl degradation, hbpC, and that
2-hydroxybiphenyl itself is the direct effector for HbpR-mediated
activation. Of several compounds tested, only the pathway
substrates 2-hydroxybiphenyl and 2,2'-dihydroxybiphenyl and
structural analogs like 2-aminobiphenyl and 2-hydroxybiphenylmethane were effectors for HbpR activation. HbpR is therefore, to our knowledge, the first regulator of the XylR/DmpR class
that recognizes biaromatic but not monoaromatic structures. Analysis of
a spontaneously occurring mutant, P. azelaica HBP1 Prp,
which can grow with the non-wild-type effector 2-propylphenol,
revealed a single mutation in the hbpR gene (T613C) leading
to a Trp
Arg substitution at amino acid residue 205. P. azelaica HBP1 derivative strains without a
functional hbpR gene constitutively expressed the genes for 2-hydroxybiphenyl degradation when complemented in trans
with the hbpR-T613C gene. This suggests the importance of
this residue, which is conserved among all members of the
XylR/DmpR subclass, for interdomain repression.
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