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Applied and Environmental Microbiology, October 2004, p. 6066-6075, Vol. 70, No. 10
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.10.6066-6075.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Genetic Analysis of Phenoxyalkanoic Acid Degradation in Sphingomonas herbicidovorans MH

Tina A. Müller,1 Steven M. Byrde,1 Christoph Werlen,1 Jan Roelof van der Meer,1,2* and Hans-Peter E. Kohler1

Swiss Federal Institute for Environmental Science and Technology (EAWAG), Dübendorf,1 Département de Microbiologie Fondamentale, BÂtiment de Biologie, University of Lausanne, Lausanne, Switzerland2

Received 2 March 2004/ Accepted 22 June 2004

Phenoxyalkanoic acid degradation is well studied in Beta- and Gammaproteobacteria, but the genetic background has not been elucidated so far in Alphaproteobacteria. We report the isolation of several genes involved in dichlor- and mecoprop degradation from the alphaproteobacterium Sphingomonas herbicidovorans MH and propose that the degradation proceeds analogously to that previously reported for 2,4-dichlorophenoxyacetic acid (2,4-D). Two genes for {alpha}-ketoglutarate-dependent dioxygenases, sdpAMH and rdpAMH, were found, both of which were adjacent to sequences with potential insertion elements. Furthermore, a gene for a dichlorophenol hydroxylase (tfdB), a putative regulatory gene (cadR), two genes for dichlorocatechol 1,2-dioxygenases (dccAI/II), two for dienelactone hydrolases (dccDI/II), part of a gene for maleylacetate reductase (dccE), and one gene for a potential phenoxyalkanoic acid permease were isolated. In contrast to other 2,4-D degraders, the sdp, rdp, and dcc genes were scattered over the genome and their expression was not tightly regulated. No coherent pattern was derived on the possible origin of the sdp, rdp, and dcc pathway genes. rdpAMH was 99% identical to rdpAMC1, an (R)-dichlorprop/{alpha}-ketoglutarate dioxygenase from Delftia acidovorans MC1, which is evidence for a recent gene exchange between Alpha- and Betaproteobacteria. Conversely, DccAI and DccAII did not group within the known chlorocatechol 1,2-dioxygenases, but formed a separate branch in clustering analysis. This suggests a different reservoir and reduced transfer for the genes of the modified ortho-cleavage pathway in Alphaproteobacteria compared with the ones in Beta- and Gammaproteobacteria.

* Corresponding author. Mailing address: Department of Fundamental Microbiology, BÂtiment de Biologie, University of Lausanne, CH-1015 Lausanne, Switzerland. Phone: 41 21 692 5630. Fax: 41 21 692 5635. E-mail: JanRoelof.VanDerMeer{at}imf.unil.ch.

Applied and Environmental Microbiology, October 2004, p. 6066-6075, Vol. 70, No. 10
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.10.6066-6075.2004
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]  
  • Liu, S., Ogawa, N., Senda, T., Hasebe, A., Miyashita, K. (2005). Amino Acids in Positions 48, 52, and 73 Differentiate the Substrate Specificities of the Highly Homologous Chlorocatechol 1,2-Dioxygenases CbnA and TcbC. J. Bacteriol. 187: 5427-5436 [Abstract] [Full Text]  


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