Dehalococcoides mccartyi strain DCMB5 Respires a broad spectrum of chlorinated aromatic compounds.
Polyhalogenated aromatic compounds are harmful environmental contaminants and tend to persist in anoxic soils and sediments. Dehalococcoides mccartyi strain DCMB5, a strain originating from dioxin-polluted river sediment, was examined for its capacity to dehalogenate diverse chloroaromatic compounds. Strain DCMB5 used hexachlorobenzenes, pentachlorobenzenes, all three tetrachlorobenzenes, and 1,2,3-trichlorobenzene as well as 1,2,3,4-tetra- and 1,2,4-trichlorodibenzo-p-dioxin as electron acceptors for organohalide respiration. In addition, 1,2,3-trichlorodibenzo-p-dioxin and 1,3-, 1,2-, and 1,4-dichlorodibenzo-p-dioxin were dechlorinated, the latter to the nonchlorinated congener with a remarkably short lag phase of 1 to 4 days following transfer. Strain DCMB5 also dechlorinated pentachlorophenol and almost all tetra- and trichlorophenols. Tetrachloroethene was dechlorinated to trichloroethene and served as an electron acceptor for growth. To relate selected dechlorination activities to the expression of specific reductive dehalogenase genes, the proteomes of 1,2,3-trichlorobenzene-, pentachlorobenzene-, and tetrachloroethene-dechlorinating cultures were analyzed. Dcmb_86, an ortholog of the chlorobenzene reductive dehalogenase CbrA, was the most abundant reductive dehalogenase during growth with each electron acceptor, suggesting its pivotal role in organohalide respiration of strain DCMB5. Dcmb_1041 was specifically induced, however, by both chlorobenzenes, whereas 3 putative reductive dehalogenases, Dcmb_1434, Dcmb_1339, and Dcmb_1383, were detected only in tetrachloroethene-grown cells. The proteomes also harbored a type IV pilus protein and the components for its assembly, disassembly, and secretion. In addition, transmission electron microscopy of DCMB5 revealed an irregular mode of cell division as well as the presence of pili, indicating that pilus formation is a feature of D. mccartyi during organohalide respiration.
Institute of Biology/Microbiology, Martin Luther University, Halle, Germany.
Marlén
M
Pöritz
Department of Proteomics, Helmholtz Centre for Environmental Research-UFZ, Leipzig, Germany.
Christian L
CL
Schiffmann
Biocentre, Martin Luther University, Halle, Germany.
Gerd
G
Hause
Institute of Biology/Microbiology, Martin Luther University, Halle, Germany.
Ulrike
U
Heinemann
Department of Proteomics, Helmholtz Centre for Environmental Research-UFZ, Leipzig, Germany.
Jana
J
Seifert
Department of Proteomics, Helmholtz Centre for Environmental Research-UFZ, Leipzig, Germany.
Nico
N
Jehmlich
Department of Proteomics, Helmholtz Centre for Environmental Research-UFZ, Leipzig, Germany Department of Metabolomics, Helmholtz Centre for Environmental Research-UFZ, Leipzig, Germany Department of Biotechnology, Chemistry and Environmental Engineering, Aalborg University, Aalborg, Denmark.
Martin
M
von Bergen
Department of Isotope Biogeochemistry, Helmholtz Centre for Environmental Research-UFZ, Leipzig, Germany.
Ivonne
I
Nijenhuis
Institute of Biology/Microbiology, Martin Luther University, Halle, Germany ute.lechner@mikrobiologie.uni-halle.de.
Ute
U
Lechner
D041862:Chloroflexi / Q000201:enzymology* / Q000378:metabolism*; D004785:Environmental Pollutants / Q000378:metabolism*; D006843:Hydrocarbons, Chlorinated / Q000378:metabolism*; D020543:Proteome / Q000032:analysis
D004785:Environmental Pollutants; D006843:Hydrocarbons, Chlorinated; D020543:Proteome