Archives of Microbiology

, Volume 155, Issue 2, pp 125–130 | Cite as

Oxidative stress responses and shock proteins in the unicellular cyanobacterium Synechococcus R2 (PCC-7942)

  • Ron Mittler
  • Elisha Tel-Or
Original Papers


Oxidative stress responses were tested in the unicellular cyanobacterium Synechococcus PCC 7942 (R2). Cells were exposed to hydrogen peroxide, cumene hydroperoxide and high light intensities. Activities of ascorbate peroxidase and catalase were correlated with the extent and time-course of oxidative stresses. Ascorbate peroxidase was found to be the major enzyme involved in the removal of hydrogen peroxide under the tested oxidative stresses. Catalase activity was inhibited in cells treated with high H2O2 concentrations, and was not induced under photo-oxidative stress. Regeneration of ascorbate in peroxide-treated cells was found to involve mainly monodehydroascorbate reductase and to a lesser extent dehydroascorbate reductase. The induction of the antioxidative enzymes was dependent on light and was inhibited by chloramphenicol. Peroxide treatment was found to induce the synthesis of eight proteins, four of which were also induced by heat shock.

Key words

Ascorbate peroxidase Catalase Ascorbate Glutathione Peroxide shock proteins Heat shock proteins Synechococcus 









reduced glutathione


oxidized glutathione


ascorbate peroxidase

DHA red.

dehydroascorbate reductase

MDA red.

monodehydroascorbate reductase

GSSG red.

glutathione reductase


heat shock proteins


peroxide shock proteins




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Copyright information

© Springer-Verlag 1991

Authors and Affiliations

  • Ron Mittler
    • 1
  • Elisha Tel-Or
    • 1
  1. 1.Department of Agricultural Botany, Faculty of AgricultureThe Hebrew University of JerusalemRehovotIsrael

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