Abstract
Prefoldin is a hexameric chaperone that has been identified in eukaryotic cells and in Archaea. E. coli cells over-expressing the prefoldin gene from the hyperthermophilic, archaeum, Pyrococcus furiosus, grew well at 48°C while control cells were unable to grow above 46°C. The isolated and purified Pfu-prefoldin (specially the β subunit and the prefoldin) thermally protected the activity of lysozyme.
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Barral JM, Broadley SA, Schaffar G, Hartl FU (2004) Roles of molecular chaperones in protein misfolding diseases. Semin Cell Dev Biol 15:17–29
Chen H, Chu Z, Zhang Y, Yang S (2006) Overexpression and characterization of the recombinant small heat shock protein from Pyrococcus furiosus. Biotechnol Lett 28:1089–1094
Chen H, Chu Z, Zhang Y, Yang S (2007) Expression and characterization of the chaperonin molecular machine from the hyperthermophilic archaeon Pyrococcus furiosus. J Basic Microbiol 47:132–137
Derlinden E, Bernaerts K, Impe JF (2008) Dynamics of Escherichia coli at elevated temperatures: effect of temperature history and medium. J Appl Microbiol 104:438–453
Ferrer M, Chernikova TN, Yakimov MM, Timmis KN (2003) Chaperonins govern growth of Escherichia coli at low temperatures. Nat Biotechnol 21:1266–1267
Garcia-Orozco KD, Lopez-Zavala AA, Puentes-Camacho D, Calderon-de-la-Barca AM, Sotelo-Mundo RR (2005) Recombinant bacterial expression of the lysozyme from the tobacco-hornworm Manduca sexta with activity at low temperatures. Biotechnol Lett 27:1075–1080
Gur E, Biran D, Gazit E, Ron EZ (2002) In vivo aggregation of a single enzyme limits growth of Escherichia coli at elevated temperatures. Mol Microbiol 46:1391–1397
Hartl FU, Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852–1858
Laksanalamai P, Pavlov AR, Slesarev AI, Robb FT (2006) Stabilization of Taq DNA Polymerase at High Temperature by Protein Folding Pathways From a Hyperthermophilic Archaeon, Pyrococcus furiosus. Biotechnol Bioeng 93:1–5
Membre JM, Leporq B, Vialette M, Mettler E, Perrier L, Thuault D, Zwietering M (2005) Temperature effect on bacterial growth rate: quantitative microbiology approach including cardinal values and variability estimates to perform growth simulation on/in food. Int J Food Microbiol 100:179–186
Okochi M, Yoshida T, Maruyama T, Kawarabayasi Y, Kikuchi H, Yohda M (2002) Pyrococcus prefoldin stabilizes protein-folding intermediates and transfers them to chaperonins for correct folding. Biochem Biophys Res Commun 291:769–774
Okochi M, Kanie K, Kurimoto M, Yohda M, Honda H (2008) Overexpression of prefoldin from hyperthermophilic archaeum Pyrococcus horokoshii OT3 endowed Escherichia coli with organic solvent tolerance. Appl Microbiol Biotechnol 79:443–449
Siegert R, Leroux MR, Scheufler C, Hartl FU, Moarefi I (2000) Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103:621–632
Soto A, Allona I, Collada C et al (1999) Heterologous expression of a plant small heat-shock protein enhances Escherichia coli viability under heat and cold stress. Plant Physiol 120:521–528
Takeuchi S (2006) Analytical assays of human HSP27 and thermal-stress survival of Escherichia coli cells that overexpress it. Biochem Biophys Res Commun 341:1252–1256
Trent DJ (1996) A review of acquired thermotolerance, heat-shock proteins, and molecular chaperones in archaea. FEMS Microbiol Rev 18:249–258
Yeh CH, Chang PFL, Yeh KW, Lin WC, Chen YM, Lin CY (1999) Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance. Proc Natl Acad Sci 94:10967–10972
Yon JM (2001) Protein folding: a perspective for biology, medicine and biotechnology. Braz J Med Biol Res 34:419–435
Young JC, Agashe VR, Siegers K, Hartl FU (2004) Pathways of chaperonemediated protein folding in the cytosol. Nat Rev Mol Cell Biol 5:781–791
Acknowledgements
This work is supported by National Basic Research Program of China (973 Program) No. 2004CB719606, 863 Program of China No. 2006AA02Z208, National Basic Research Program of China (973 Program) No. 2007CB714304, National Basic Research Program of China (973 Program) No. 2007CB707804 and the Key Project of CAS Knowledge Innovation Program KSC2-YW-G-005.
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Chen, H., Yang, L., Zhang, Y. et al. Over-expression and characterization of recombinant prefoldin from hyperthermophilic archaeum Pyrococcus furiosus in E. coli . Biotechnol Lett 32, 429–434 (2010). https://doi.org/10.1007/s10529-009-0156-5
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DOI: https://doi.org/10.1007/s10529-009-0156-5