Proteomic signatures uncover thiol-specific electrophile resistance mechanisms in Bacillus subtilis

Haike Antelmann, Michael Hecker, Peter Zuber

Research output: Contribution to journalReview article

36 Scopus citations

Abstract

Proteomic and transcriptomics signatures are powerful tools for visualizing global changes in gene expression in bacterial cells after exposure to stress, starvation or toxic compounds. Based on the global expression profile and the dissection into specific regulons, this knowledge can be used to predict the mode of action for novel antimicrobial compounds. This review summarizes our recent progress of proteomic signatures in the model bacterium for low-GC Gram-positive bacteria Bacillus subtilis in response to the antimicrobial compounds phenol, catechol, salicylic acid, 2-methylhydroquinone (2-MHQ) and 6-brom-2-vinyl-chroman-4-on (chromanon). Catechol, 2-MHQ and diamide displayed a common mode of action, as revealed by the induction of the thiol-specific oxidative stress response. In addition, multiple dioxygenases/glyoxalases, azoreductases and nitroreductases were induced by thiol-reactive compounds that are regulated by two novel thiol-specific regulators, YodB and MhqR (YkvE), both of which contribute to electrophile resistance in B. subtilis. These novel thiol-stress-responsive mechanisms are highly conserved among Gram-positive bacteria and are thought to have evolved to detoxify quinone-like electrophiles.

Original languageEnglish (US)
Pages (from-to)77-90
Number of pages14
JournalExpert Review of Proteomics
Volume5
Issue number1
DOIs
StatePublished - Feb 1 2008

Keywords

  • Bacillus subtilis
  • Electrophile resistance
  • MhqR
  • Proteomic signature
  • Thiol
  • YodB

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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