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Civil and Environmental Engineering, Cornell University, Ithaca, New York 14853,1 Department of Microbiology, Cornell University, Ithaca, New York 14853,2 Proteomic and Mass Spectrometry, Cornell University, Ithaca, New York 14853,3 Environmental Engineering and Science, Clemson University, Clemson, South Carolina 296344
Received 8 September 2006/ Accepted 29 October 2006
Anaerobic reductive dehalogenation by Dehalococcoides spp. is an ideal system for studying functional diversity of closely related strains of bacteria. In Dehalococcoides spp., reductive dehalogenases (RDases) are key respiratory enzymes involved in the anaerobic detoxification of halogenated compounds at contaminated sites globally. Although housekeeping genes sequenced from Dehalococcoides spp. are >85% identical at the amino acid level, different strains are capable of dehalogenating diverse ranges of compounds, depending largely on the suite of RDase genes that each strain harbors and expresses. We identified RDase proteins that corresponded to known functions in four characterized cultures and predicted functions in an uncharacterized Dehalococcoides-containing mixed culture. Homologues within RDase subclusters containing PceA, TceA, and VcrA were among the most frequently identified proteins. Several additional proteins, including a formate dehydrogenase-like protein (Fdh), had high coverage in all strains and under all growth conditions.
Published ahead of print on 10 November 2006.
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