Abstract
Problem statement: Glutaredoxins (GRXs) are ubiquitous small heat stable glutathione-dependent oxidoreductase enzymes that play a crucial role in plant development and response to oxidative stress. Approach: Cyanobacterium Synechocystis strain PCC 6803 contains two genes (slr1562 and ssr2061) encoding glutaredoxins. In the present investigation the slr1562 gene (grxC) was isolated and characterized. Results: The results revealed that the amino acid sequence deduced from GrxC protein share high identity with those of GRXs from other organisms and contain the consensus GRX family domain with a CPFC active site. Northern blotting analysis revealed that the expression of slr1562 gene could be induced by oxidative and salt stresses. Moreover, the protein GrxC was successfully overexpressed as a soluble fraction in Escherichia coli JM109. The over-expression of GrxC in Escherichia coli cells significantly increased resistance of cells to oxidative, drought and salt stresses. Conclusion/Recommendations: These results suggest that the slr1562 gene could play an important role in regulating abiotic tolerance against oxidative, drought and salt stresses in different organisms.
Highlights
Glutaredoxins (Grx; EC 1.20.4.1) are glutathione dependent oxidoreductase proteins with a small (10-12 kDa) molecular weight
We demonstrated that the over expression of the protein Grx2 encoded by ssr2061 in E. coli cells showed high tolerance to NaCl compared to cells transformed with the vector alone (Gaber et al, 2006)
For the construction of the plasmid to express slr1562 gene, the plasmid was digested with NdeI and BamH1 and the resultant 330 bp DNA fragment was cloned into a pET3a vector (Novagen, Madison, NI, USA) digested with the same restriction enzymes
Summary
Glutaredoxins (Grx; EC 1.20.4.1) are glutathione dependent oxidoreductase proteins with a small (10-12 kDa) molecular weight. AtGRXcp (AT3G54900), the first characterized CGFS intensities were investigated, the cells at log-phase stage type Grx in plants, was found to suppress the sensitivity of yeast grx cells to H2O2 and protein oxidation and function in early seedling growth under H2O2 stress were transferred to 4 oC under dim light intensity (30 μE m−2 s−1) and harvested at the times given previously. The fern PvGRX5 was reported to increase plant tolerance to arsenic, high temperature and oxidative stresses (Sundaram et al, 2007; 2009; Sundaram and Rathinasabapathi, 2010) Taken together, these studies suggest that plant Grxs have diverse functions in plant. We demonstrated that the over expression of the protein Grx encoded by ssr2061 in E. coli cells showed high tolerance to NaCl compared to cells transformed with the vector alone (Gaber et al, 2006).
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