Abstract

Sphingomonas wittichii RW1 is a bacterium of interest due to its ability to degrade polychlorinated dioxins, which represent priority pollutants in the USA and worldwide. Although its genome has been fully sequenced, many questions exist regarding changes in protein expression of S. wittichii RW1 in response to dioxin metabolism. We used difference gel electrophoresis (DIGE) and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) to identify proteomic changes induced by growth on dibenzofuran, a surrogate for dioxin, as compared to acetate. Approximately 10% of the entire putative proteome of RW1 could be observed. Several components of the dioxin and dibenzofuran degradation pathway were shown to be upregulated, thereby highlighting the utility of using proteomic analyses for studying bioremediation agents. This is the first global protein analysis of a microorganism capable of utilizing the carbon backbone of both polychlorinated dioxins and dibenzofurans as the sole source for carbon and energy.

Original languageEnglish (US)
Article number408690
JournalJournal of Biomedicine and Biotechnology
Volume2012
DOIs
StatePublished - 2012

Fingerprint

Sphingomonas
Dioxins
Proteomics
Bacteria
Carbon
Environmental Biodegradation
Bioremediation
Protein S
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Proteome
Electrophoresis
Metabolism
Microorganisms
Ionization
Mass spectrometry
Desorption
Proteins
Acetates
Genes
Gels

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Medicine
  • Genetics
  • Molecular Biology
  • Health, Toxicology and Mutagenesis
  • Medicine(all)

Cite this

Proteomic profiling of the dioxin-degrading bacterium sphingomonas wittichii RW1. / Colquhoun, David R.; Hartmann, Erica M.; Halden, Rolf.

In: Journal of Biomedicine and Biotechnology, Vol. 2012, 408690, 2012.

Research output: Contribution to journalArticle

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