Proteomic analysis of Burkholderia cepacia MBA4 in the degradation of monochloroacetate

Proteomics. 2007 Apr;7(7):1107-16. doi: 10.1002/pmic.200600660.

Abstract

Burkholderia cepacia MBA4 is a bacterium that degrades 2-haloacids by removing the halogen and subsequent metabolism of the product for energy. In this study, 2-DE, MS/MS, and N-terminal amino acid sequencing were used to investigate the protein expression profiles of MBA4 grown in a 2-haloacid (monochloroacetate, MCA) and in the corresponding metabolic product (glycolate). Glycolate was used as a control to eliminate the proteins induced by it. Five proteins were found to be up-regulated and five proteins were down-regulated in response to MCA. The differentially expressed proteins were examined, seven of them were identified by MS/MS and two of them were sequenced by Edman degradation. Our results definitely provide an insight for understanding the physiology of B. cepacia MBA4 in response to organohalide contaminated site.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetates / metabolism*
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Burkholderia cepacia / chemistry*
  • Burkholderia cepacia / genetics
  • Burkholderia cepacia / metabolism*
  • Electrophoresis, Gel, Two-Dimensional
  • Gene Expression Regulation, Bacterial
  • Glycolates / metabolism
  • Molecular Sequence Data
  • Proteomics*
  • Tandem Mass Spectrometry

Substances

  • Acetates
  • Bacterial Proteins
  • Glycolates
  • glycolic acid
  • chloroacetic acid