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Journal of Bacteriology, August 1999, p. 4568-4575, Vol. 181, No. 15
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

areABC Genes Determine the Catabolism of Aryl Esters in Acinetobacter sp. Strain ADP1

Rheinallt M. Jones,1 Lauren S. Collier,2 Ellen L. Neidle,2 and Peter A. Williams1,*

School of Biological Sciences, University of Wales Bangor, Bangor, Gwynedd LL57 2UW, Wales, United Kingdom,1 and Department of Microbiology, University of Georgia, Athens, Georgia 30602-26052

Received 30 March 1999/Accepted 27 May 1999

Acinetobacter sp. strain ADP1 is able to grow on a range of esters of aromatic alcohols, converting them to the corresponding aromatic carboxylic acids by the sequential action of three inducible enzymes: an areA-encoded esterase, an areB-encoded benzyl alcohol dehydrogenase, and an areC-encoded benzaldehyde dehydrogenase. The are genes, adjacent to each other on the chromosome and transcribed in the order areCBA, were located 3.5 kbp upstream of benK. benK, encoding a permease implicated in benzoate uptake, is at one end of the ben-cat supraoperonic cluster for benzoate catabolism by the beta -ketoadipate pathway. Two open reading frames which may encode a transcriptional regulator, areR, and a porin, benP, separate benK from areC. Each are gene was individually expressed to high specific activity in Escherichia coli. The relative activities against different substrates of the cloned enzymes were, within experimental error, identical to that of wild-type Acinetobacter sp. strain ADP1 grown on either benzyl acetate, benzyl alcohol, or 4-hydroxybenzyl alcohol as the carbon source. The substrate preferences of all three enzymes were broad, encompassing a range of substituted aromatic compounds and in the case of the AreA esterase, different carboxylic acids. The areA, areB, and areC genes were individually disrupted on the chromosome by insertion of a kanamycin resistance cassette, and the rates at which the resultant strains utilized substrates of the aryl ester catabolic pathway were severely reduced as determined by growth competitions between the mutant and wild-type strains.

* Corresponding author. Mailing address: School of Biological Sciences, University of Wales Bangor, Bangor, Gwynedd LL57 2UW, Wales, United Kingdom. Phone: (44) 1248 382363. Fax: (44) 1248 370731. E-mail: P.A.Williams{at}bangor.ac.uk.

Journal of Bacteriology, August 1999, p. 4568-4575, Vol. 181, No. 15
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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