Functional characterization of osmotically inducible protein C (MG_427) from Mycoplasma genitalium

Wenbo Zhang, Joel B. Baseman

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Mycoplasma genitalium is the smallest self-replicating bacterium and an important human pathogen responsible for a range of urogenital infections and pathologies. Due to its limited genome size, many genes conserved in other bacteria are missing in M. genitalium. Genes encoding catalase and superoxide dismutase are absent, and how this pathogen overcomes oxidative stress remains poorly understood. In this study, we characterized MG_427, a homolog of the conserved osmC, which encodes hydroperoxide peroxidase, shown to protect bacteria against oxidative stress. We found that recombinant MG_427 protein reduced organic and inorganic peroxide substrates. Also, we showed that a deletion mutant of MG_427 was highly sensitive to killing by tert-butyl hydroperoxide and H2O2 compared to the sensitivity of the wild type. Further, the fully complemented mutant strain reversed its oxidative sensitivity. Examination of the expression pattern of MG_427 during osmotic shock, oxidative stress, and other stress conditions revealed its lack of induction, distinguishing MG_427 from other previously characterized osmC genes.

Original languageEnglish (US)
Pages (from-to)1012-1019
Number of pages8
JournalJournal of Bacteriology
Volume196
Issue number5
DOIs
StatePublished - Mar 2014

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Mycoplasma genitalium
Protein C
Oxidative Stress
Bacteria
Genes
tert-Butylhydroperoxide
Genome Size
Osmotic Pressure
Peroxides
Catalase
Hydrogen Peroxide
Peroxidase
Superoxide Dismutase
Pathology
Infection
Proteins

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

Functional characterization of osmotically inducible protein C (MG_427) from Mycoplasma genitalium. / Zhang, Wenbo; Baseman, Joel B.

In: Journal of Bacteriology, Vol. 196, No. 5, 03.2014, p. 1012-1019.

Research output: Contribution to journalArticle

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