Acknowledgement
Supported by : Rural Development Administration
References
- Ackerley, D.F., Barak, Y., Lynch, S.V., Curtin, J., and Matin, A. (2006). Effect of chromate stress on Escherichia coli K-12. J. Bacteriol. 188, 3371-3381 https://doi.org/10.1128/JB.188.9.3371-3381.2006
- Benov, L., and Al-Ibraheem, J. (2002). Disrupting Escherichia coli: a comparison of methods. J. Biochem. Mol. Biol. 35, 428-431 https://doi.org/10.5483/BMBRep.2002.35.4.428
- Bernstein, C., Bernstein, H., Payne, C.M., Beard, S.E., and Schneider, J. (1999). Bile salt activation of stress response promoters in Escherichia coli. Curr. Microbiol. 39, 68-72 https://doi.org/10.1007/s002849900420
- Bucheler, U.S., Werner, D., and Schirmer, R.H. (1992). Generating compatible translation initiation regions for heterologous gene expression in Escherichia coli by exhaustive periShine-Dalgarno mutagenesis. Human glutathione reductase cDNA as a model. Nucleic Acids Res. 20, 3127-3133 https://doi.org/10.1093/nar/20.12.3127
- Carmel-Harel, O., and Storz, G. (2000). Roles of the glutathioneand thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu. Rev. Microbiol. 54, 439-461 https://doi.org/10.1146/annurev.micro.54.1.439
- Castro, F.A., Herdeiro, R.S., Panek, A.D., Eleutherio, E.C., and Pereira, M.D. (2007). Menadione stress in Saccharomyces cerevisiae strains deficient in the glutathione transferases. Biochim. Biophys. Acta 1770, 213-220 https://doi.org/10.1016/j.bbagen.2006.10.013
- Chen, J., Brevet, A., Fromant, M., Leveque, F., Schmitter, J.M., Blanquet, S., and Plateau, P. (1990). Pyrophosphatase is essential for growth of Escherichia coli. J. Bacteriol. 172, 5686-5689 https://doi.org/10.1128/jb.172.10.5686-5689.1990
- Chou, J.H., Greenberg, J.T., and Demple, B. (1993). Posttranscriptional repression of Escherichia coli OmpF protein in response to redox stress: positive control of the micF antisense RNA by the soxRS locus. J. Bacteriol. 175, 1026-1031 https://doi.org/10.1128/jb.175.4.1026-1031.1993
- Collinson, L.P., and Dawes, I.W. (1995). Isolation, characterization and overexpression of the yeast gene, GLR1, encoding glutathione reductase. Gene 156, 123-127 https://doi.org/10.1016/0378-1119(95)00026-3
- Creissen, G.P., and Mullineaux, P.M. (1995). Cloning and characterisation of glutathione reductase cDNAs and identification of two genes encoding the tobacco enzyme. Planta 197, 422-425
- Fan, W., Zhang, Z., and Zhang, Y. (2009). Cloning and molecular characterization of fructose-1,6-bisphosphate aldolase gene regulated by high-salinity and drought in Sesuvium portulacastrum. Plant Cell Rep. 28, 975-984 https://doi.org/10.1007/s00299-009-0702-6
- Greer, S., and Perham, R.N. (1986). Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases. Biochemistry 25, 2736-2742 https://doi.org/10.1021/bi00357a069
- Han, K.Y., Park, J.S., Seo, H.S., Ahn, K.Y., and Lee, J. (2008). Multiple stressor-induced proteome responses of Escherichia coli BL21(DE3). J. Proteome Res. 7, 1891-1903 https://doi.org/10.1021/pr700631c
- Huang, Y.J., Tsai, T.Y., and Pan, T.M. (2007). Physiological response and protein expression under acid stress of Escherichia coli O157:H7 TWC01 isolated from Taiwan. J. Agric. Food Chem. 55, 7182-7191 https://doi.org/10.1021/jf071014s
- Jiang, Z.Y., Hunt, J.V., and Wolff, S.P. (1992). Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in low density lipoprotein. Anal. Biochem. 202, 384-389 https://doi.org/10.1016/0003-2697(92)90122-N
- Jiang, F., Hellman, U., Sroga, G.E., Bergman, B., and Mannervik, B. (1995). Cloning, sequencing, and regulation of the glutathione reductase gene from the cyanobacterium Anabaena PCC 7120. J. Biol. Chem. 270, 22882-22889 https://doi.org/10.1074/jbc.270.39.22882
- Kubo, A., Sano, T., Saji, H., Tanaka, K., Kondo, N., and Tanaka, K. (1993). Primary structure and properties of glutathione reductase from Arabidopsis thaliana. Plant Cell Physiol. 34, 1259-1266
- Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 https://doi.org/10.1038/227680a0
- Lee, H., Jo, J., and Son, D. (1998). Molecular cloning and characterization of the gene encoding glutathione reductase in Brassica campestris. Biochim. Biophys. Acta 1395, 309-314 https://doi.org/10.1016/S0167-4781(97)00198-X
- Lee, H., Won, S.H., Lee, B.H., Park, H.D., Chung, W.I., and Jo, J. (2002). Genomic cloning and characterization of glutathione reductase gene from Brassica campestris var. pekinensis. Mol. Cells 13, 245-251
- Li, M., Huang, W., Yang, Q., Liu, X., and Wu, Q. (2005). Expression and oxidative stress tolerance studies of glutaredoxin from cyanobacterium Synechocystis sp. PCC 6803 in Escherichia coli. Protein Expr. Purif. 42, 85-91 https://doi.org/10.1016/j.pep.2005.03.027
- Martelli, A., and Moulis, J.M. (2004). Zinc and cadmium specifically interfere with RNA-binding activity of human iron regulatory protein 1. J. Inorg. Biochem. 98, 1413-1420 https://doi.org/10.1016/j.jinorgbio.2004.04.011
- Mendoza-Cozatl, D., Loza-Tavera, H., Hernandez-Navarro, A., and Moreno-Sanchez, R. (2005). Sulfur assimilation and glutathione metabolism under cadmium stress in yeast, protists and plants. FEMS Microbiol. Rev. 29, 653-671 https://doi.org/10.1016/j.femsre.2004.09.004
- Mishra, Y., Chaurasia, N., and Rai, L.C. (2009). AhpC (alkyl hydroperoxide reductase) from Anabaena sp. PCC 7120 protects Escherichia coli from multiple abiotic stresses. Biochem. Biophys. Res. Commun. 381, 606-611 https://doi.org/10.1016/j.bbrc.2009.02.100
- Mockett, R.J., Sohal, R.S., and Orr, W.C. (1999). Overexpression of glutathione reductase extends survival in transgenic Drosophila melanogaster under hyperoxia but not normoxia. FASEB J. 13, 1733-1742 https://doi.org/10.1096/fasebj.13.13.1733
- Nellemann, L.J., Holm, F., Atlung, T., and Hansen, F.G. (1989). Cloning and characterization of the Escherichia coli phosphoglycerate kinase (pgk) gene. Gene 77, 185-191 https://doi.org/10.1016/0378-1119(89)90373-9
- Nishino, K., Honda, T., and Yamaguchi, A. (2005). Genome-wide analyses of Escherichia coli gene expression responsive to the BaeSR two-component regulatory system. J. Bacteriol. 187, 1763-1772 https://doi.org/10.1128/JB.187.5.1763-1772.2005
- O’Donovan, D.J., Katkin, J.P., Tamura, T., Husser, R., Xu, X., Smith, C.V., and Welty, S.E. (1999). Gene transfer of mitochondrially targeted glutathione reductase protects H441 cells from t-butyl hydroperoxide-induced oxidant stresses. Am. J. Respir. Cell Mol. Biol. 20, 256-263 https://doi.org/10.1165/ajrcmb.20.2.3367
- Perry, A.C., Ni Bhriain, N., Brown, N.L., and Rouch, D.A. (1991). Molecular characterization of the gor gene encoding glutathione reductase from Pseudomonas aeruginosa: determinants of substrate specificity among pyridine nucleotide-disulphide oxidoreductases. Mol. Microbiol. 5, 163-171 https://doi.org/10.1111/j.1365-2958.1991.tb01837.x
- Pilon-Smits, E.A., Zhu, Y.L., Sears, T., and Terry, N. (2000). Overexpression of glutathion reductase in Brassica juncea: effects on cadmium accumulation and tolerance. Physiol. Plant 110, 455-460 https://doi.org/10.1111/j.1399-3054.2000.1100405.x
- Seaver, L.C., and Imlay, J.A. (2001). Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J. Bacteriol. 183, 7173-7181 https://doi.org/10.1128/JB.183.24.7173-7181.2001
-
Seo, J.S., Lee, K.W., Rhee, J.S., Hwang, D.S., Lee, Y.M., Park, H.G., and Park, J.S. (2006). Environmental stressors (salinity, heavy metals,
$H_2O_2$ ) modulate expression of glutathione reductase (GR) gene from the intertidal copepod Tigriopus japonicus. Aquatic Toxiol. 80, 281-289 https://doi.org/10.1016/j.aquatox.2006.09.005 - Spickett, C.M., Smirnoff, N., and Pitt, A.R. (2000). The biosynthesis of erythroascorbate in Saccharomyces cerevisiae and its role as an antioxidant. Free Radic Biol Med 28, 183-192 https://doi.org/10.1016/S0891-5849(99)00214-2
- Stevens, R.G., Creissen, G.P., and Mullineaux, P.M. (2000). Characterisation of pea cytosolic glutathione reductase expressed in transgenic tobacco. Planta 211, 537-545 https://doi.org/10.1007/s004250000304
- Sugiyama, K., Kawamura, A., Izawa, S., and Inoue, Y. (2000). Role of glutathione in heat-shock-induced cell death of Saccharomyces cerevisiae. Biochem. J. 352, 71-78 https://doi.org/10.1042/0264-6021:3520071
- Tamarit, J., Cabiscol, E., and Ros, J. (1998). Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J. Biol. Chem. 273, 3027-3032 https://doi.org/10.1074/jbc.273.5.3027
- Wheeler, G.L., and Grant, C.M. (2004). Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae. Physiol. Plant 120, 12-20 https://doi.org/10.1111/j.0031-9317.2004.0193.x
- Yohannes, E., Barnhart, D.M., and Slonczewski, J.L. (2004). pHdependent catabolic protein expression during anaerobic growth of Escherichia coli K-12. J. Bacteriol. 186, 192-199 https://doi.org/10.1128/JB.186.1.192-199.2004
- Yoon, H.S., Lee, I.A., Lee, H., Lee, B.H., and Jo, J. (2005). Overexpression of a eukaryotic glutathione reductase gene from Brassica campestris improved resistance to oxidative stress in Escherichia coli. Biochem. Biophys. Res. Commun. 326, 618-623 https://doi.org/10.1016/j.bbrc.2004.11.095
- Yu, J., and Zhou, C.Z. (2007). Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae. Proteins 68, 972-979 https://doi.org/10.1002/prot.21354
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