Induction of DnaK upon <i>γ</i>-Irradiation at High and Low Rates in <i>Escherichia coli</i>
- 1 Food Research and Development Centre, Agriculture and Agri-Food Canada, Saint-Hyacinthe, Québec, Canada
- 2 Food Research and Development Centre, Agriculture and Agri-Food Canada, Saint-Hyacinthe, Québec, Canada
- 3 Département des sciences animales, Faculté des sciences de l’agriculture et de l’alimentation, Université Laval, Québec, Québec, Canada
- 4 Food Research and Development Centre, Agriculture and Agri-Food Canada, Saint-Hyacinthe, Québec, Canada
Abstract
DnaK is implicated in protein folding, repair and degradation. Its protective role during heat shock is well documented and many other stresses can also induce its production. Using a competitive ELISA, intracellular DnaK concentrations were determined in Escherichia coli ATCC 25922 exposed to a γ-irradiation dose of 0.3 KGy applied either at high (8 × 10 -2 KGy/min) or low rates (3 × 10 -3 KGy/min) and with or without a recuperation period of 22 h at 37℃ post-treatment. All four irradiation treatments reduced cell counts similarly and significantly compared to the control (P < 0.0001). However, the highest DnaK concentration was observed in cells irradiated at low rate without recuperation (105,416 molecules/cell; P = 0.0001). Furthermore, DnaK levels remained higher than the control (38,500 molecules/ cell) after the recuperation period (P < 0.05). Variation in the intracellular DnaK concentration indicates that the bacterial stress response was modulated differently according to the irradiation treatment (P = 0.0001).
- K. Turgay, “Role of Proteolysis and Chaperones in Stress Response and Regulation,” In: G. Storz and R. Hengge, Eds., Bacterial Stress Response, 2nd Edition, ASM Press, Washington DC, 2011, pp. 75-90.
- G. Storz and R. Hengge-Aronis, “Bacterial Stress Response,” 2nd Edition, ASM Press, Washington DC, 2011.
- K. Seyer, M. Lessard, G. Piette, M. Lacroix and L. Saucier, “Escherichia coli Heat Shock Protein DnaK: Production and Its Consequences in Terms of Monitoring Cooking,” Applied and Environmental Microbiology, Vol. 69, No. 6, 2003, pp. 3231-3237. doi:10.1128/AEM.69.6.3231-3237.2003
- M.-J. Lemay, N. Rodrigue, C. Gariépy and L. Saucier, “Adaptation of Lactobacillus alimentarius to Environmental Stresses,” International Journal of Food Microbiology, Vol. 55, No. 1-3, 2000, pp. 249-253. doi:10.1016/S0168-1605(00)00181-1
- W. A. Houry, “Chaperone-Assisted Protein Folding in the Cell Cytoplasm,” Current Protein & Peptide Science, Vol. 2, No. 3, 2001, pp. 227-244. doi:10.2174/1389203013381134
- S. Zietkiewicz, A. Lewandowska, P. Stockiand and K. Liberek, “Hsp70 Chaperone Machine Remodels Protein Aggregates at the Initial Step of Hsp70-Hsp100-Dependent Disaggregation,” Journal of Biological Chemistry, Vol. 281, No. 11, 2006, pp. 7022-7029. doi:10.1074/jbc.M507893200
- T. Yura, M. Kanemori and M. T. Morita, “The Heat Shock Response: Regulation and Function,” In: G. Storz and R. Hengge, Eds., Bacterial Stress Response, ASM Press, Washington DC, 2000, pp. 75-90.
- C. Georgopoulos and W. J. Welch, “Role of the Major Heat Shock Proteins as Molecular Chaperones,” Annual Review of Cell and Developmental Biology, Vol. 9, 1993, pp. 601-634. doi:10.1146/annurev.cb.09.110193.003125
- F. C. Neidhardt, R. A. Vanbogelen and V. Vaughn, “The Genetics and Regulation of Heat-Shock Proteins,” Annual Review of Genetics, Vol. 18, 1984, pp. 295-329. doi:10.1146/annurev.ge.18.120184.001455
- S. H. Park, S. J. Lee, H. Y. Chung, T. H. Kim, C. K. Cho, S. Y. Yoo and Y. S. Lee, “Inducible Heat-Shock Protein 70 Is Involved in the Radioadaptive Response,” Radiation Research, Vol. 153, No. 3, 2000, pp. 318-326. doi:10.1667/0033-7587(2000)153[0318:IHSPII]2.0.CO;2
- S. Caillet, M. Millette, D. Dussault, F. Shareck and M. Lacroix, “Effect of Gamma Radiation on Heat Shock Protein Expression of Four Foodborne Pathogens,” Journal of Applied Microbiology, Vol. 105, No. 5, 2008, pp. 1384-1391. doi:10.1111/j.1365-2672.2008.03891.x