Abstract

BackgroundThe Copper/Zinc superoxide dismutase (Cu/ZnSOD) gene, SOD gene, was isolated from a Deschampsia antarctica Desv. by cDNA library screening. The expression of SOD gene in the leaves of D. antarctica was determined by RT-PCR and its differential expression of gene transcripts in conditions of cold and UV radiation stresses was revealed by northern blot.FindingsThe molecular characterization shows that SOD cDNA is 709 bp in length, which translates an ORF of 152 amino acids that correspond to a protein of predicted molecular mass of 15 kDa. The assay shows that the expression of SOD gene increases when D. antarctica is acclimatised to 4°C and exposed to UV radiation. These results indicate that the SOD gene of D. antarctica is involved in the antioxidative process triggered by oxidative stress induced by the conditions of environmental change in which they live.ConclusionThe present results allow us to know the characteristics of Cu/ZnSOD gene from D. antarctica and understand that its expression is regulated by cold and UV radiation.

Highlights

  • The Copper/Zinc superoxide dismutase (Cu/ZnSOD) gene, Superoxide dismutase (SOD) gene, was isolated from a Deschampsia antarctica Desv. by cDNA library screening

  • The present results allow us to know the characteristics of Cu/ZnSOD gene from D. antarctica and understand that its expression is regulated by cold and UV radiation

  • We describe the molecular characterization of the Cu/ZnSOD gene of D. antarctica and analyzed their expression under stress conditions at low temperatures and exposure to UV radiation

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Summary

Introduction

The Copper/Zinc superoxide dismutase (Cu/ZnSOD) gene, SOD gene, was isolated from a Deschampsia antarctica Desv. by cDNA library screening. The Copper/Zinc superoxide dismutase (Cu/ZnSOD) gene, SOD gene, was isolated from a Deschampsia antarctica Desv. The expression of SOD gene in the leaves of D. antarctica was determined by RT-PCR and its differential expression of gene transcripts in conditions of cold and UV radiation stresses was revealed by northern blot. Superoxide dismutase (SOD; EC 1.15.1.1) is a ubiquitous enzyme belonging to a family of metalloenzymes, which catalyze the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. The reaction is continued by catalase (CAT) and ascorbate peroxidase (APX), converting the hydrogen peroxide to water and molecular oxygen, preventing the formation of hydroxyl radicals, which are highly destructive to the cell [1,2]. The enzyme SOD is considered the first-line defense because it catalyses the first reaction in the system harvesting oxygen-free radicals [3]. The Cu/ZnSOD is generally found in the chloroplasts, the (page number not for citation purposes)

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