Genetic analysis of phenoxyalkanoic acid degradation in Sphingomonas herbicidovorans MH.
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, sdpA(MH) and rdpA(MH), 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 (dccA(I/II)), two for dienelactone hydrolases (dccD(I/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. rdpA(MH) was 99% identical to rdpA(MC1), an (R)-dichlorprop/alpha-ketoglutarate dioxygenase from Delftia acidovorans MC1, which is evidence for a recent gene exchange between Alpha- and Betaproteobacteria. Conversely, DccA(I) and DccA(II) 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.
Müller
Tina A
TA
Swiss Federal Institute for Environmental Science and Technology, Dübendorf, Switzerland.
Byrde
Steven M
SM
Werlen
Christoph
C
van der Meer
Jan Roelof
JR
Kohler
Hans-Peter E
HP
D015084:2,4-Dichlorophenoxyacetic Acid / Q000378:metabolism; D008456:2-Methyl-4-chlorophenoxyacetic Acid / Q000031:analogs & derivatives* / Q000378:metabolism; D001483:Base Sequence; D001673:Biodegradation, Environmental; D020118:Cupriavidus necator / Q000235:genetics / Q000378:metabolism; D004269:DNA, Bacterial / Q000235:genetics; D049308:Dioxygenases / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D019143:Evolution, Molecular; D005798:Genes, Bacterial; D006016:Glycolates / Q000378:metabolism*; D006540:Herbicides / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000235:genetics / Q000378:metabolism; D008954:Models, Biological; D008969:Molecular Sequence Data; D005810:Multigene Family; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D020578:Sphingomonas / Q000235:genetics* / Q000378:metabolism*
D004269:DNA, Bacterial; D006016:Glycolates; D006540:Herbicides; D011994:Recombinant Proteins; D015084:2,4-Dichlorophenoxyacetic Acid; C008340:mecoprop; D008456:2-Methyl-4-chlorophenoxyacetic Acid; D006899:Mixed Function Oxygenases; D049308:Dioxygenases; C044173:chlorocatechol 1,2-dioxygenase