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Isocitrate lyase of the facultative intracellular pathogen Rhodococcus equi^a

Department of Industrial Microbiology, Conway Institute of Biomolecular and Biomedical Sciences, University College Dublin, Dublin 4, and Dublin Molecular Medicine Centre, Dublin, Ireland¹

Author for correspondence: Wim G. Meijer. Tel: +353 1 716 1364. Fax: +353 1 716 1183. e-mail: wim.meijer{at}ucd.ie

Isocitrate lyase is the first enzyme of the glyoxylate shunt which is required for the assimilation of fatty acids and acetate. The intracellular pathogen Rhodococcus equi contains high activities of this enzyme following growth on acetate and lactate, indicating that it plays an important role in the metabolism of these substrates. The gene encoding isocitrate lyase (aceA) was cloned and sequenced. It specifies a 46846 Da protein, which was shown to be functional by expressing it in Escherichia coli. A gene similar to fadB, encoding 3-hydroxyacyl-CoA dehydrogenase, was located 90 bp downstream from aceA. Northern hybridization and RT-PCR experiments showed that aceA and fadB are cotranscribed into a 2·8 kb transcript. A smaller 1·6 kb aceA transcript was also observed which was 2·5-fold more abundant than the aceA-fadB transcript. It is proposed that a stable hairpin structure with a free energy (G) of -28·5 kcal mol^-1 and located in the 90 bp aceA-fadB intergenic region is involved in stabilizing the aceA transcript.

Keywords: aceA, fadB, lactate and acetate metabolism, glyoxylate shunt, mRNA processing

^a The GenBank accession number for the sequence reported in this paper is AY044917.

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