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J Bacteriol, May 1998, p. 2493-2501, Vol. 180, No. 9
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Regulation of Benzoate Degradation in
Acinetobacter sp. Strain ADP1 by BenM, a LysR-Type
Transcriptional Activator
Lauren S.
Collier,1
George L.
Gaines III,2 and
Ellen L.
Neidle1,*
Department of Microbiology, University of
Georgia, Athens, Georgia 30602-2605,1 and
Isogenetics, Inc., Chicago, Illinois 606122
Received 24 October 1997/Accepted 27 February 1998
In Acinetobacter sp. strain ADP1, benzoate degradation
requires the ben genes for converting benzoate to catechol
and the cat genes for degrading catechol. Here we describe
a novel transcriptional activator, BenM, that regulates the chromosomal
ben and cat genes. BenM is homologous to CatM,
a LysR-type transcriptional activator of the cat genes.
Unusual regulatory features of this system include the abilities of
both BenM and CatM to recognize the same inducer, cis,cis-muconate, and to regulate some of the
same genes, such as catA and catB. Unlike CatM,
BenM responded to benzoate. Benzoate together with
cis,cis-muconate increased the BenM-dependent
expression of the benABCDE operon synergistically. CatM was
not required for this synergism, nor did CatM regulate the expression
of a chromosomal benA::lacZ
transcriptional fusion. BenM-mediated regulation differs significantly
from that of the TOL plasmid-encoded conversion of benzoate to catechol
in pseudomonads. The benM gene is immediately upstream of,
and divergently transcribed from, benA, and a possible DNA
binding site for BenM was identified between the two coding regions.
Two mutations in the predicted operator/promoter region rendered
ben gene expression either constitutive or inducible by
cis,cis-muconate but not benzoate. Mutants
lacking BenM, CatM, or both of these regulators degraded aromatic
compounds at different rates, and the levels of intermediary
metabolites that accumulated depended on the genetic background. These
studies indicated that BenM is necessary for ben gene
expression but not for expression of the cat genes, which
can be regulated by CatM. In a catM-disrupted strain, BenM
was able to induce higher levels of catA expression than
catB expression.
*
Corresponding author. Mailing address: Department of
Microbiology, University of Georgia, 527 Biological Sciences Building, Athens, GA 30602-2605. Phone: (706) 542-2852. Fax: (706) 542-2674. E-mail: eneidle{at}uga.cc.uga.edu.
J Bacteriol, May 1998, p. 2493-2501, Vol. 180, No. 9
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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