Archives of Microbiology

, Volume 192, Issue 6, pp 447–459

Oxidative stress protection and the repair response to hydrogen peroxide in the hyperthermophilic archaeon Pyrococcus furiosus and in related species

Authors

  • Kari R. Strand
    • Department of Biochemistry and Molecular BiologyUniversity of Georgia
    • Department of Molecular BiosciencesUniversity of Oslo
  • Chengjun Sun
    • Department of Biochemistry and Molecular BiologyUniversity of Georgia
  • Ting Li
    • Department of Biochemistry and Molecular BiologyUniversity of Georgia
  • Francis E. JenneyJr.
    • Department of Biochemistry and Molecular BiologyUniversity of Georgia
    • Department of Basic SciencesGeorgia Campus Philadelphia College of Osteopathic Medicine
  • Gerrit J. Schut
    • Department of Biochemistry and Molecular BiologyUniversity of Georgia
    • Department of Biochemistry and Molecular BiologyUniversity of Georgia
Original Paper

DOI: 10.1007/s00203-010-0570-z

Cite this article as:
Strand, K.R., Sun, C., Li, T. et al. Arch Microbiol (2010) 192: 447. doi:10.1007/s00203-010-0570-z

Abstract

Pyrococcus furiosus is a shallow marine, anaerobic archaeon that grows optimally at 100°C. Addition of H2O2 (0.5 mM) to a growing culture resulted in the cessation of growth with a 2-h lag before normal growth resumed. Whole genome transcriptional profiling revealed that the main response occurs within 30 min of peroxide addition, with the up-regulation of 62 open reading frames (ORFs), 36 of which are part of 10 potential operons. More than half of the up-regulated ORFs are of unknown function, while some others encode proteins that are involved potentially in sequestering iron and sulfide, in DNA repair and in generating NADPH. This response is thought to involve primarily damage repair rather than protection, since cultures exposed to sub-toxic levels of H2O2 were not more resistant to the subsequent addition of H2O2 (0.5–5.0 mM). Consequently, there is little if any induced protective response to peroxide. The organism maintains a constitutive protective mechanism involving high levels of oxidoreductase-type enzymes such as superoxide reductase, rubrerythrin, and alkyl hydroperoxide reductase. Related hyperthermophiles contain homologs of the proteins involved in the constitutive protective mechanism but these organisms were more sensitive to peroxide than P. furiosus and lack several of its peroxide-responsive ORFs.

Keywords

HyperthermophileAnaerobicOxidative stressPeroxide response

Supplementary material

203_2010_570_MOESM1_ESM.pdf (425 kb)
(PDF 425 kb)

Copyright information

© Springer-Verlag 2010