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RADIATION EFFECTS OF HSP EXPRESSION IN E COLI

Effect of γ-irradiation on gene expression of heat shock proteins in the foodborne pathogen Escherichia coli O157:H7

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Pages 268-273 | Received 03 Jun 2013, Accepted 17 Oct 2013, Published online: 06 Feb 2014

References

  • Acebron SP, Martin I, del Castillo U, Moro F, Muga A. 2009. DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface. FEBS Lett 583:2991–2996.
  • Banatvala N, Griffin PM, Greene KD, Barrett TJ, Bibb WF, Green JH, Wells JG. 2001. The United States National Prospective Hemolytic Uremic Syndrome Study: Microbiologic, serologic, clinical, and epidemiologic findings. J Infect Dis 183:1063–1070.
  • Barends TR, Werbeck ND, Reinstein J. 2010. Disaggregases in 4 dimensions. Curr Op Struct Biol 20:46–53.
  • Bergholz TM, Wick LM, Qi W, Riordan JT, Ouellette LM, Whittam TS. 2007. Global transcriptional response of Escherichia coli O157:H7 to growth transitions in glucose minimal medium. BMC Microbiol 7:97.
  • Bissonnette SA, Rivera-Rivera I, Sauer RT, Baker TA. 2010. The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease. Molec Microbiol 75:1539–1549.
  • Bukau B. 1993. Regulation of the Escherichia coli heat-shock response. Molec Microbiol 9:671–680.
  • Caillet S, Shareck F, Lacroix M. 2005. Effect of gamma radiation and oregano essential oil on murein and ATP concentration of Escherichia coli O157:H7. J Food Protect 68:2571–2579.
  • Caillet S, Millette M, Dussault D, Shareck F, Lacroix M. 2008. Effect of gamma radiation on heat shock protein expression of four foodborne pathogens. J Appl Microbiol 105:1384–1391.
  • Carruthers MD, Minion C. 2009. Transcriptome analysis of Escherichia coli O157:H7 EDL933 during heat shock. FEMS Microbiol Lett 295:96–102.
  • Chaudhuri TK, Verma VK, Maheshwari A. 2009. GroEL assisted folding of large polypeptide substrates in Escherichia coli: Present scenario and assignments for the future. Prog Biophys Molec Biol 99:42–50.
  • De Maio A. 1999. Heat shock proteins: Facts, thoughts, and dreams. Shock 11(1):1–12.
  • Feder ME, Hofmann GE. 1999. Heat-shock proteins, molecular chaperones, and the stress response: Evolutionary and ecological physiology. Ann Rev Physiol 61:243–282.
  • Ferens WA, Hovde CJ. 2011. Escherichia coli O157:H7: Animal reservoir and sources of human infection. Foodborne Path Dis 8(4):465–487.
  • Genest O, Hoskins JR, Camberg JL, Doyle SM, Wickner S. 2011. Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling. Proc Nat Acad Sci USA 108:8206–8211.
  • Hasan CM, Shimizu K. 2008. Effect of temperature up-shift on fermentation and metabolic characteristics in view of gene expressions in Escherichia coli. Microbial Cell Factories 7:35.
  • Kornitzer D, Teff D, Altuvia S, Oppenheim AB. 1991. Isolation, characterization, and sequence of an Escherichia coli heat shock gene, htpX. J Bacteriol 173:2944–2953.
  • Livak KJ, Schmittgen TD. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods: Companion to Methods in Enzymol 25: 402–408.
  • Matuszewska M, Kuczynska-Wisnik D, Laskowska E, Liberek K. 2005. The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state. J Biologic Chem 280:12292–12298.
  • Monk JD, Beuchat LR, Doyle MP. 1995. Irradiation inactivation of food-borne microorganisms. J Food Protect 58:197–208.
  • Morita M, Kanemori M, Yanagi H, Yura T. 1999. Heat-induced synthesis of sigma32 in Escherichia coli: Structural and functional dissection of rpoH mRNA secondary structure. J Bacteriol 181: 401–410.
  • Sakoh M, Ito K, Akiyama Y. 2005. Proteolytic activity of HtpX, a membrane-bound and stress-controlled protease from Escherichia coli. J Biol Chem 280(39):33305–33310.
  • Schlesinger MJ. 1990. Heat shock proteins. J Biologic Chem 265: 12111–12114.
  • Schroder H, Langer T, Hartl FU, Bukau B. 1993. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J 12:4137–144.
  • Siegenthaler RK, Christen P. 2006. Tuning of DnaK chaperone action by nonnative protein sensor DnaJ and thermosensor GrpE. J Biologic Chem 281:34448–34456.
  • Sugimoto S, Saruwatari K, Higashi C, Sonomoto K. 2008. The proper ratio of GrpE to DnaK is important for protein quality control by the DnaK-DnaJ-GrpE chaperone system and for cell division. Microbiology 154:1876–1885.
  • Veinger L, Diamant S, Buchner J, Goloubinoff P. 1998. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J Biologic Chem 273:11032–11037.
  • Wood OB, Bruhn CM. 2000. Position of the American Dietetic Association: Food irradiation. J Am Dietetic Assoc 100:246–253.
  • Yura T, Kanemori M, Morita MY. 2000. The heat shock response: Regulation and function. In: Storz G, Hengge-Aronis R, editors. Bacterial stress responses. Washington: ASM Press. pp. 3–18.
  • Zhaohui X, Sigler PB. 1998. GroEL/GroES: Structure and function of a two-stroke folding machine. J Struct Biol 124:129–1141.
  • Zolkiewski M. 2006. A camel passes through the eye of a needle: Protein unfolding activity of Clp ATPases. Molec Microbiol 61: 1094–1100.

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