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(Received for publication, September 6, 1996, and in revised form, October 28, 1996)
From the Centro Nacional de Biotecnología, Consejo Superior
de Investigaciones Científicas, Campus de Cantoblanco,
28049 Madrid, Spain
This work reports a genetic analysis of the
interactions between NahR, the LysR-type regulator of the NAH operons
for biodegradation of naphthalene in Pseudomonas, and its
aromatic effectors. Six mutants encoding NahR variants responsive to
salicylate analogs such as benzoate, which is not an inducer for the
wild type regulator, were isolated with a polymerase chain
reaction-based saturation mutagenesis protocol. Most mutants displaying
a specific change of effector profile bore single amino acid
substitutions within a short protein segment of 60 residues located at
the central portion of the NahR sequence. Some of the protein variants
exhibited an increased affinity for salicylate and also for otherwise
suboptimal effectors, with apparent
Ks
Volume 272, Number 7,
Issue of February 14, 1997
pp. 3986-3992
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
values 5-100-fold
lower than those of the wild type NahR protein. In addition, all
mutants were activated by inducers bearing novel substituents at
positions 1 or 2 of the aromatic ring and displayed also an enhanced
tolerance to changes at positions 3 and 4. Correlation between
mutations in NahR and the structures of the new effectors suggested
that protein sites Met116, Arg132,
Asn169, and Arg248 are involved in effector
recognition and binding during the earlier steps of the process leading
to transcriptional activation of cognate NAH promoters.
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