Genetic analysis of phenoxyalkanoic acid degradation in Sphingomonas herbicidovorans MH.

Détails

ID Serval
serval:BIB_2B24F71A659B
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Genetic analysis of phenoxyalkanoic acid degradation in Sphingomonas herbicidovorans MH.
Périodique
Applied and Environmental Microbiology
Auteur(s)
Müller T.A., Byrde S.M., Werlen C., van der Meer J.R., Kohler H.P.
ISSN
0099-2240 (Print)
ISSN-L
0099-2240
Statut éditorial
Publié
Date de publication
2004
Volume
70
Numéro
10
Pages
6066-6075
Langue
anglais
Résumé
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.
Mots-clé
2,4-Dichlorophenoxyacetic Acid/metabolism, 2-Methyl-4-chlorophenoxyacetic Acid/analogs & derivatives, 2-Methyl-4-chlorophenoxyacetic Acid/metabolism, Base Sequence, Biodegradation, Environmental, Cupriavidus necator/genetics, Cupriavidus necator/metabolism, DNA, Bacterial/genetics, Dioxygenases/genetics, Dioxygenases/metabolism, Escherichia coli/genetics, Evolution, Molecular, Genes, Bacterial, Glycolates/metabolism, Herbicides/metabolism, Mixed Function Oxygenases/genetics, Mixed Function Oxygenases/metabolism, Models, Biological, Molecular Sequence Data, Multigene Family, Recombinant Proteins/genetics, Recombinant Proteins/metabolism, Sphingomonas/genetics, Sphingomonas/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
21/01/2008 13:35
Dernière modification de la notice
20/08/2019 13:10
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