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

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Abstract

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.

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Abbreviations

ASC:

ascorbate

DHA:

dehydroascorbate

MDA:

monodehydroascorbate

GSH:

reduced glutathione

GSSG:

oxidized glutathione

ASC Per:

ascorbate peroxidase

DHA red.:

dehydroascorbate reductase

MDA red.:

monodehydroascorbate reductase

GSSG red.:

glutathione reductase

HSP:

heat shock proteins

PSP:

peroxide shock proteins

Cm :

chloramphenicol

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Authors and Affiliations

  1. Department of Agricultural Botany, Faculty of Agriculture, The Hebrew University of Jerusalem, P. O. Box 12, 76100, Rehovot, Israel

    Ron Mittler & Elisha Tel-Or

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  1. Ron Mittler
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  2. Elisha Tel-Or
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Mittler, R., Tel-Or, E. Oxidative stress responses and shock proteins in the unicellular cyanobacterium Synechococcus R2 (PCC-7942). Arch. Microbiol. 155, 125–130 (1991). https://doi.org/10.1007/BF00248605

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