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Applied and Environmental Microbiology, September 2004, p. 5357-5365, Vol. 70, No. 9
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.9.5357-5365.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Localization and Characterization of Two Novel Genes Encoding Stereospecific Dioxygenases Catalyzing 2(2,4-Dichlorophenoxy)propionate Cleavage in Delftia acidovorans MC1

Kathleen M. Schleinitz,1 Sabine Kleinsteuber,1* Tatiana Vallaeys,2,3 and Wolfgang Babel1

Department of Environmental Microbiology, UFZ Centre for Environmental Research Leipzig-Halle, Leipzig, Germany,1 Institut National de la Recherche Agronomique,2 Laboratoire de Génomique des Microorganismes Pathogène, Institut Pasteur, Paris, France3

Received 11 March 2004/ Accepted 20 May 2004

Two novel genes, rdpA and sdpA, encoding the enantiospecific {alpha}-ketoglutarate dependent dioxygenases catalyzing R,S-dichlorprop cleavage in Delftia acidovorans MC1 were identified. Significant similarities to other known genes were not detected, but their deduced amino acid sequences were similar to those of other {alpha}-ketoglutarate dioxygenases. RdpA showed 35% identity with TauD of Pseudomonas aeruginosa, and SdpA showed 37% identity with TfdA of Ralstonia eutropha JMP134. The functionally important amino acid sequence motif HX(D/E)X23-26(T/S)X114-183HX10-13R/K, which is highly conserved in group II {alpha}-ketoglutarate-dependent dioxygenases, was present in both dichlorprop-cleaving enzymes. Transposon mutagenesis of rdpA inactivated R-dichlorprop cleavage, indicating that it was a single-copy gene. Both rdpA and sdpA were located on the plasmid pMC1 that also carries the lower pathway genes. Sequencing of a 25.8-kb fragment showed that the dioxygenase genes were separated by a 13.6-kb region mainly comprising a Tn501-like transposon. Furthermore, two copies of a sequence similar to IS91-like elements were identified. Hybridization studies comparing the wild-type plasmid and that of the mutant unable to cleave dichlorprop showed that rdpA and sdpA were deleted, whereas the lower pathway genes were unaffected, and that deletion may be caused by genetic rearrangements of the IS91-like elements. Two other dichlorprop-degrading bacterial strains, Rhodoferax sp. strain P230 and Sphingobium herbicidovorans MH, were shown to carry rdpA genes of high similarity to rdpA from strain MC1, but sdpA was not detected. This suggested that rdpA gene products are involved in the degradation of R-dichlorprop in these strains.

* Corresponding author. Mailing address: UFZ Centre for Environmental Research Leipzig-Halle, Department of Environmental Microbiology, Permoserstr. 15, 04318 Leipzig, Germany. Phone: 49-341-235-2191. Fax: 49-341-235-2247. E-mail: sabine.kleinsteuber{at}ufz.de.

Applied and Environmental Microbiology, September 2004, p. 5357-5365, Vol. 70, No. 9
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.9.5357-5365.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Muller, T. A., Fleischmann, T., van der Meer, J. R., Kohler, H.-P. E. (2006). Purification and Characterization of Two Enantioselective {alpha}-Ketoglutarate-Dependent Dioxygenases, RdpA and SdpA, from Sphingomonas herbicidovorans MH.. Appl. Environ. Microbiol. 72: 4853-4861 [Abstract] [Full Text]  


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