Rubrerythrin and peroxiredoxin: two novel putative peroxidases in the hydrogenosomes of the microaerophilic protozoon Trichomonas vaginalis

Mol Biochem Parasitol. 2005 Aug;142(2):212-23. doi: 10.1016/j.molbiopara.2005.04.003.

Abstract

The parasitic flagellate Trichomonas vaginalis contains hydrogenosomes, anaerobic organelles related to mitochondria, that generate ATP from the fermentative conversion of pyruvate to acetate, CO2 and molecular hydrogen. Although an essentially anaerobic organism, Trichomonas encounters low oxygen concentrations in its natural habitat and has to protect itself, and especially the oxygen-sensitve enzymes of hydrogenosomal metabolism, from oxidative damage. We have identified two novel proteins in the hydrogenosomal proteome with strong similarity to two putative prokaryotic peroxidases, rubrerythrin and periplasmic thiol peroxidase. Both proteins have previously been found in many prokaryotes but were not known from eukaryotes, suggesting a significant prokaryotic component in the oxygen-detoxification system of trichomonad hydrogenosomes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins
  • Ferredoxins
  • Hemerythrin
  • Hydrogen / metabolism*
  • Molecular Sequence Data
  • Organelles / enzymology*
  • Oxidative Stress
  • Oxygen / pharmacology
  • Peroxidases / chemistry
  • Peroxidases / genetics
  • Peroxidases / metabolism*
  • Peroxiredoxins
  • Phylogeny
  • Proteome
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism*
  • Rubredoxins
  • Sequence Alignment
  • Trichomonas vaginalis / enzymology*
  • Trichomonas vaginalis / genetics
  • Trichomonas vaginalis / physiology

Substances

  • Bacterial Proteins
  • Ferredoxins
  • Hemerythrin
  • Proteome
  • Protozoan Proteins
  • Rubredoxins
  • rubrerythrins
  • Hydrogen
  • Peroxidases
  • Peroxiredoxins
  • Oxygen