Superoxide dismutase (SOD)-deficient Escherichia coli OX326Acells are protected against chemically-induced oxidative stress by expression of the chaperonin GroESL. This protection is equivalent to expression of superoxide dismutase even though GroESL has no inherent SOD activity. Co-overexpression of GroESL and SOD in the same cells results in higher protein yields of SOD and greater metallation of SOD when compared with expression of SOD alone. Greater metallation results in the higher specific activity of SOD that is observed in heat shock, and is not due to increased synthesis of SOD mRNA or protein.
Bull, C. and Fee, J.A. (1985) Steady-state kinetic studies of superoxide dismutases: Properties of the iron containing protein from Escherichia coli. Journal of the American Chemical Society, 107, 3295-3304. http://dx.doi.org/10.1021/ja00297a040
Sakamoto, H. and Touati, D. (1984) Cloning of the iron superoxide dismutase gene (sodB) in Escherichia coli K-12. Journal of Bacteriology, 159, 418-420.
Carlioz, A., Ludwig, M.L., Stallings, W.C., Fee, J.A., Steinman, H. M. and Touati, D. (1988) Iron Superoxide Dismutase: Nucleotide Sequence of the gene from Escherichia coli K12 and correlations with crystal structures. The Journal of Biological Chemistry, 263, 1555-1562.
Touati, D. (1983) Cloning and mapping of the manganese superoxide dismutase gene (sodA) of Escherichia coli K-12. Journal of Bacteriology, 155, 1078-1087.
McCord, J.M. and Fridovich, I. (1969) Superoxide dismutase: An enzymic function for erythrocuprein (Hemocuprein). The Journal of Biological Chemistry, 244, 6049-6055.
Edwards, R.A., Baker, H.M., Jameson, G.B., Whittaker, M.M., Whittaker, J.W. and Baker, E.N. (1998) Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1 Å resolution. Journal of Biological Inorganic Chemistry, 3, 161-171. http://dx.doi.org/10.1007/s007750050217
Lah, M.S., Dixon, M.M., Pattridge, K.A., Stallings, W.C., Fee, J. A. and Ludwig, M. L. (1995) Structure-function in Escherichia coli iron superoxide dismutase: Comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry, 34, 1646-1660. http://dx.doi.org/10.1021/bi00005a021
Hunter, T., Bannister, J.V. and Hunter, G.J. (2002) Thermostability of manganese- and iron-superoxide dismutases from Escherichia coli is determined by the characteristic position of a glutamine residue. European Journal of Biochemistry, 269, 5137-5148. http://dx.doi.org/10.1046/j.1432-1033.2002.03200.x
Ose, D.E. and Fridovich, I. (1979) Manganese-containing superoxide dismutase from Escherichia coli: Reversible resolution and metal replacements. Archives of Biochemistry and Biophysics, 194, 360-364. http://dx.doi.org/10.1016/0003-9861(79)90628-3
Beyer, W.F. and Fridovich, I. (1991) In vivo competition between iron and manganese for the occupancy of the active site region of the manganese-superoxide dismutase of Escherichia coli. The Journal of Biological Chemistry, 266, 303-308.
Steinman, H.M., Weinstein, L. and Brenowitz, M. (1994) The manganese superoxide dismutase of Escherichia coli K-12 associates with DNA. The Journal of Biological Chemistry, 269, 28629-28634.
Hopkin, K.A., Papazian, M.A. and Steinman, H.M. (1992) Functional differences between manganese and iron superoxide dismutases in Escherichia coli K-12. The Journal of Biological Chemistry, 267, 24253-24258.
Hassan, H.M. and Fridovich, I. (1977) Regulation of the synthesis of superoxide dismutase in Escherichia coli. The Journal of Biological Chemistry, 252, 7667-7672.
Hassan, H.M. and Fridovich, I. (1977) Enzymatic defenses against the toxicity of oxygen and of streptonigrin. Journal of Bacteriology, 129, 1574.
Greenberg, J.T. and Demple, B. (1989) A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress. Journal of Bacteriology, 171, 3933-3939.
Compan, I. and Touati, D. (1993) Interaction of Six Global Transcriptional Regulators in Expression of Manganese Dismutase in Escherichia coli K-12. Journal of Bacteriology, 175, 1687-1696.
Ellis, R.J. and Hartl, F.U. (1996) Protein folding in the cell: Competing models of chaperonin function. The FASEB Journal, 10, 20-26.
Hartl, F. U. (1996) Molecular chaperones in cellular protein folding, Nature, 381, 571-579. http://dx.doi.org/10.1038/381571a0
Fayet, O., Ziegelhoffer, T. and Georgopoulos, C. (1989) The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. Journal of Bacteriology, 171, 1379-1385.
Sigler, P.B., Xu, Z., Rye, H.S., Burston, S.G., Fenton, W. A. and Horwich, A. L. (1998) Structure and function in GroEL-mediated protein folding. Annual Review of Biochemistry, 67, 581-608. http://dx.doi.org/10.1146/annurev.biochem.67.1.581
Houry, W.A., Frishman, D., Eckerskorn, C., Lottspeich, F. and Hartl, F.U. (1999) Identification of in vivo substrates of the chaperonin GroEL. Nature, 402, 147-154. http://dx.doi.org/10.1038/45977
Lee, P.C., Bochner, B.R. and Ames, B.N. (1983) AppppA, heat-shock stress, and cell oxidation. Proceedings of the National Academy of Sciences USA, 80, 7496-7500. http://dx.doi.org/10.1073/pnas.80.24.7496
Benov, L. and Fridovich, I. (1995) Superoxide dismutase protects against aerobic heat shock in Escherichia coli, Journal of Bacteriology, 177, 3344-3346.
Privalle, C.T. and Fridovich, I. (1987) Induction of superoxide dismutase in Escherichia coli by heat shock, Proceedings of the National Academy of Sciences USA, 84, 2723-2726. http://dx.doi.org/10.1073/pnas.84.9.2723
Hassan, H.M. and Lee, F.J. (1989) Effect of temperature and htpR on the biosynthesis of superoxide dismutase in Escherichia coli. FEMS Microbiology Letters, 58, 133-137. http://dx.doi.org/10.1111/j.1574-6968.1989.tb03033.x
Christman, M.F., Morgan, R.W., Jacobson, F.S. and Ames, B.N. (1985) Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell, 41, 753-762. http://dx.doi.org/10.1016/S0092-8674(85)80056-8
Demple, B. and Amabile-Cuevas, C.F. (1991) Redox redux: The control of oxidative stress responses. Cell, 67, 837-839. http://dx.doi.org/10.1016/0092-8674(91)90355-3
Tsaneva, I.R. and Weiss, B. (1990) soxR, a locus governing a superoxide response regulon in Escherichia coli K-12. Journal of Bacteriology, 172, 4197-205.
Walkup, L.K. and Kogoma, T. (1989) Escherichia coli proteins inducible by oxidative stress mediated by the superoxide radical. Journal of Bacteriology, 171, 1476-1484.
Yamamori, T. and Yura, T. (1982) Genetic control of heat-shock protein synthesis and its bearing on growth and thermal resistance in Escherichia coli K-12. Proceedings of the National Academy of Sciences USA, 79, 860-864. http://dx.doi.org/10.1073/pnas.79.3.860
Grossman, A.D., Erickson, J.W. and Gross, C.A. (1984) The htpR gene product of E. coli is a sigma factor for heat-shock promoters. Cell, 38, 383-390. http://dx.doi.org/10.1016/0092-8674(84)90493-8
VanBogelen, R.A., Kelley, P.M. and Neidhardt, F.C. (1987) Differential induction of heat shock, SOS, and oxidation stress regulons and accumulation of nucleotides in Escherichia coli. Journal of Bacteriology, 169, 26-32.
Amrein, K.E., Takacs, B., Stieger, M., Molnos, J., Flint, N. A. and Burn, P. (1995) Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL. Proceedings of the National Academy of Sciences USA, 92, 1048-1052. http://dx.doi.org/10.1073/pnas.92.4.1048
Hunter, T. and Hunter, G.J. (1998) GST fusion protein expression vector for in-frame cloning and sitedirected mutagenesis. BioTechniques, 24, 194-196.
Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular cloning: A laboratory manual. 2nd Edition, Cold Spring Harbor Laboratory, Cold Spring Harbour, NY.
Bradford, M.M. (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilising the principle of protein binding. Analytical Biochemistry, 72, 248-254. http://dx.doi.org/10.1016/0003-2697(76)90527-3
Laemmli, U. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685. http://dx.doi.org/10.1038/227680a0
McCord, J.M. and Fridovich, I. (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). The Journal of Biological Chemistry, 244, 6049-6055.
Ysebaert-Vanneste, M. and Vanneste, W.H. (1980) Quantitative resolution of Cu, Zn-and Mn-superoxide dismutase activities. Analytical Biochemistry, 107, 86-95. http://dx.doi.org/10.1016/0003-2697(80)90496-0
Beauchamp, C. and Fridovich, I. (1971) Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels. Analytical Biochemistry, 44, 276-287. http://dx.doi.org/10.1016/0003-2697(71)90370-8
Clark, E.D.B. (1998) Refolding of recombinant proteins. Current Opinion in Biotechnology, 9, 157-163. http://dx.doi.org/10.1016/S0958-1669(98)80109-2
Farewell, A. and Neidhardt, F.C. (1998) Effect of temperature on in vivo protein synthetic capacity in Escherichia coli. Journal of Bacteriology, 180, 4704-4710.
Begonia, G.B. and Salin, M.L. (1991) Elevation of superoxide dismutase in Halobacterium halobium by heat shock. Journal of Bacteriology, 173, 5582-5584.
Lilie, H. and Buchner, J. (1995) Interaction of GroEL with a highly structured folding intermediate: Iterative binding cycles do not involve unfolding. Proceedings of the National Academy of Sciences of the United States of America, 92, 8100-8104. http://dx.doi.org/10.1073/pnas.92.18.8100
Reverter-Branchat, G., Cabiscol, E., Tamarit, J. and Ros, J. (2004) Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: Common targets and prevention by calorie restriction. The Journal of Biological Chemistry, 279, 31983-31989. http://dx.doi.org/10.1074/jbc.M404849200
Cabiscol, E., Piulats, E., Echave, P., Herrero, E. and Ros, J. (2000) Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. The Journal of Biological Chemistry, 275, 27393-37398.
Csermely, P. (1999) Chaperone-percolator model: A possible molecular mechanism of Anfinsen-cage-type chaperones. Bioessays, 21, 959-965. http://dx.doi.org/10.1002/(SICI)1521-1878(199911)21:11 3.0.CO;2-1
Luk, E., Carroll, M., Baker, M. and Culotta, V. C. (2003) Manganese activation of superoxide dismutase 2 in Saccharomyces cerevisiae requires MTM1, a member of the mitochondrial carrier family. Proceedings of the National Academy of Sciences of the United States of America, 100, 10353-10357. http://dx.doi.org/10.1073/pnas.1632471100