References
- Abdul, K., Terada, K., Gotoh, T., Hafizur, R. and Mori, M. (2002) Characterization and functional analysis of a heart-enriched DnaJ/ Hsp40 homolog dj4/DjA4. Cell Stress Chap. 7, 156-166. https://doi.org/10.1379/1466-1268(2002)007<0156:CAFAOA>2.0.CO;2
- Brehmer, D., Rudiger, S., Gässler, C. S., Klostermeier, D., Packschies, L., Reinstein, J., Mayer, M. P. and Bukau, B. (2001) Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange. Nat. Struct. Biol. 8, 427-432. https://doi.org/10.1038/87588
- Bukau, B. and Horwich, A. L. (1999) The Hsp70 and Hsp60 chaperone machines. Cell 692, 351-366.
- Cho, E. K. and Hong, C. B. (2004) Molecular cloning and expression pattern analyses of heat shock protein 70 genes from Nicotiana tabacum. J. Plant Biol. 47, 149-159. https://doi.org/10.1007/BF03030646
- Cho, E. K., Lee, Y. K. and Hong, C. B. (2005) A Cyclophilin from Griffithsia japonica has thermoprotective activity and is affected by CsA. Mol. Cells 20, 142-150.
- Efremova, S. M., Margulis, B. A., Guzhova, I. V., Itskovich, V. B., Lauenroth, S., Muller, W. E. and Schroder, H. C. (2002) Heat shock protein hsp70 expression and DNA damage in Baikalian sponges exposed to model pollutants and wastewater from Baikalsk Pulp and Paper Plant. Aquat. Toxicol. 57, 267-280. https://doi.org/10.1016/S0166-445X(01)00209-0
- Groemping, Y. and Reinstein, J. (2001) Folding properties of the nucleotide exchanger factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response. J. Mol. Biol. 314, 167-178. https://doi.org/10.1006/jmbi.2001.5116
- Hartl, F. U. and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: From nascent chain to folded protein. Science 295, 1852-1858. https://doi.org/10.1126/science.1068408
- Haslbeck, M., Miess, A., Stromer, T., Walter, S. and Buchner, J (2005) Disassembling protein aggregates in the yeast cytosol; The cooperation of HSP26 with SSA1 and HSP104. J. Biol. Chem. 280, 23861-23868. https://doi.org/10.1074/jbc.M502697200
- Hoff, K. G., Silberg, J. J. and Vickery, L. E. (2000) Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/ Hsc20 molecular chaperone system of Escherichia coli. Proc. Natl. Acad. Sci. USA 97, 7790-7795. https://doi.org/10.1073/pnas.130201997
- Kelley, W. L. (1999) Molecular chaperones: How J domains turn on Hsp70s. Curr. Biol. 22, 305-308.
- Kluck, C. J., Patzelt, H., Genevaux, P., Brehmer, D., Rist, W., Schneider-Mergener, J., Bukau, B. and Mayer, B. P. (2002) Structure-function analysis of HscC, the Escherichia coli member of a novel subfamily of specialized Hsp70 chaperones. J. Biol. Chem. 277, 41060-41069. https://doi.org/10.1074/jbc.M206520200
- Lee, G. J. and Vierling, E. (2000) A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein. Plant Physiol. 122, 189-198. https://doi.org/10.1104/pp.122.1.189
- Lee, S. Y. and Tsai, F. T. F. (2005) Molecular chaperones in protein quality control. J. Biochem. Mol. Biol. 38, 259-265. https://doi.org/10.5483/BMBRep.2005.38.3.259
- Liu, J. G., Yao, Q. H., Zhang, Z., Peng, R. H., Xiong, A. S., Xu, F. and Zhu, H. (2005) Isolation and characterization of a cDNA encoding two novel heat-shock factor OsHSF6 and OsHSF12 in Oryza Sativa L. J. Biochem. Mol. Biol. 38, 602-608. https://doi.org/10.5483/BMBRep.2005.38.5.602
- Luft, J. C. and Dix, D. J. (1999) HSP70 expression and function during embryogenesis. Cell Stress Chap. 4, 162-170. https://doi.org/10.1379/1466-1268(1999)004<0162:HEAFDE>2.3.CO;2
- Mayer, M. P., Brehmer, D., Gassler, C. S. and Bukau, B. (2001) Advances in protein chemistry: Protein folding in the cell. Acad. Press 59, 1-44.
- Mayer, M. P. and Bukau, B. (2005) Hsp70 chaperones: Cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62, 670-684. https://doi.org/10.1007/s00018-004-4464-6
- Mayer, M. P., Rudiger, S. and Bukau, B. (2000) Molecular basis of interactions of the DnaK chaperone with substrates. Biol. Chem. 381, 877-885. https://doi.org/10.1515/BC.2000.109
- Michels, A. A., Kanon, B., Bensaude, O., Konings, A. W. T. and Kampinga, H. H. (1997) HSP70 and HSP40 chaperone activities in the cytoplasm and the nucleus of mammalian cells. J. Biol. Chem. 272, 33283-33289. https://doi.org/10.1074/jbc.272.52.33283
- Mogk, A., Tomoyasu, T., Goloubinoff, P., Rudiger, S., Roder, D., Langen, H. and Bukau, B. (1999) Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18, 6934-6949. https://doi.org/10.1093/emboj/18.24.6934
- Nollen, E. A. A., Brunsting, J. F., Roelofsen, H., Weber, L. A. and Kampinga, H. H. (1999) In vivo chaperone activity of heat shock protein 70 and thermotolerance. Mol. Cell. Biol. 19, 2069-2079. https://doi.org/10.1128/MCB.19.3.2069
- Sambrook, J., Fritsch, E. F. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nded. Cold Spring Harbor Laboratory Press, New York.
- Silberg, J. J. and Vickery, L. E. (2000) Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli. J. Biol. Chem. 275, 7779-7786. https://doi.org/10.1074/jbc.275.11.7779
- Silberg, J. J., Tapley, T. L., Hoff. K. G. and Vickery, L. E. (2004) Regulation of the HscA ATPase reaction cycle by the cochaperone HscB and the iron-sulfur cluster assembly protein IscU. J. Biol. Chem. 279, 53924-53931. https://doi.org/10.1074/jbc.M410117200
- Tanaka, N., Nakao, S., Wadai, H., Ikeda, S., Chatellier, J. and Kunugi, S. (2002) The substrate binding domain of DnaK facilitates slow protein refolding. Proc. Natl. Acad. Sci. USA 99, 15398-15403. https://doi.org/10.1073/pnas.242317099
-
Tatsuta, T., Tomoyasu, T., Bukau, B., Kitagawa, M., Mori, H., Karata, K. and Ogura, T. (1998) Heat shock regulation in the ftsH null mutant of Escherichia coli: Dissection of stability and activity control mechanisms of
$\sigma^{32}$ in vivo. Mol. Microbiol. 30, 583-593. https://doi.org/10.1046/j.1365-2958.1998.01091.x - Tomoyasu, T., Mogk, A., Langen, H., Goloubinoff, P. and Bukau, B. (2001) Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol. Microbiol. 40, 397-413. https://doi.org/10.1046/j.1365-2958.2001.02383.x
- Tuttle, A. M. (2006) Characterization of the expression and function of Rana catesbeiana HSP30 and Xenopus laevis HSP27. M.S. thesis. University of Waterloo, Ontario.
- Veinger, L., Diamant, S., Buchner, J. and Goloubinoff, P. (1998) The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J. Biol. Chem. 273, 11032-11037. https://doi.org/10.1074/jbc.273.18.11032
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