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ID: 334050.0, MPI für molekulare Genetik / Department of Vertebrate Genomics
Identification of a chlorobenzene reductive dehalogenase in dehalococcoides sp. strain CBDB1
Authors:Adrian, Lorenz; Rahnenführer, Jan; Gobom, Johan; Hölscher, Tina
Date of Publication (YYYY-MM-DD):2007-12
Title of Journal:Applied and Environmental Microbiology
Journal Abbrev.:Appl Environ Microbiol
Issue / Number:23
Start Page:7717
End Page:7724
Copyright:© 2007, American Society for Microbiology
Review Status:not specified
Audience:Experts Only
Abstract / Description:A chlorobenzene reductive dehalogenase of the anaerobic dehalorespiring bacterium Dehalococcoides sp. strain CBDB1 was identified. Due to poor biomass yields, standard protein isolation procedures were not applicable. Therefore, cell extracts from cultures grown on trichlorobenzenes were separated by native polyacrylamide gel electrophoresis and analyzed directly for chlorobenzene reductive dehalogenase activity within gel fragments. Activity was found in a single band, even though electrophoretic separation was performed under aerobic conditions. Matrix-assisted laser desorption ionization mass spectrometry (MALDI MS) and nano-liquid chromatography-MALDI MS analysis of silver-stained replicas of the active band on native polyacrylamide gels identified a protein product of the cbdbA84 gene, now called cbrA. The cbdbA84 gene is one of 32 reductive dehalogenase homologous genes present in the genome of strain CBDB1. The chlorobenzene reductive dehalogenase identified in our study represents a member of the family of corrinoid/iron-sulfur cluster-containing reductive dehalogenases. No orthologs of cbdbA84 were found in the completely sequenced genomes of Dehalococcoides sp. strains 195 and BAV1 nor among the genes amplified from Dehalococcoides sp. strain FL2 or mixed cultures containing Dehalococcoides. Another dehalogenase homologue (cbdbA80) was expressed in cultures that contained 1,2,4-trichlorobenzene, but its role is unclear. Other highly expressed proteins identified with our approach included the major subunit of a protein annotated as formate dehydrogenase, transporter subunits, and a putative S-layer protein.
External Publication Status:published
Document Type:Article
Communicated by:Hans Lehrach
Affiliations:MPI für molekulare Genetik
External Affiliations:Fachgebiet Technische Biochemie, Institut für Biotechnologie, Technische Universität Berlin, 13353 Berlin, Germany
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