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Volumn 80, Issue 6, 2002, Pages 797-809

The oligomeric state, complex formation, and chaperoning activity of Hsp70 and Hsp80 of Neurospora crassa

Author keywords

Citrate synthase; Dynamic light scattering; Molecular chaperones; Neurospora crassa; Surface plasmon resonance; Trypsin digestion

Indexed keywords

CELLS; LIGHT SCATTERING; OLIGOMERS; PROTEINS; SURFACE PLASMON RESONANCE;

EID: 0142164883     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o02-166     Document Type: Article
Times cited : (6)

References (52)
  • 1
    • 0029037015 scopus 로고
    • Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication
    • Buchberger, A., Theyssen, H., Schröder, H., McCarty, J.S., Virgallita, G., Milkereit, P., Reinstein, J., and Bukau, B. 1995. Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J. Biol. Chem. 270: 16 903 - 16 910.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16903-16910
    • Buchberger, A.1    Theyssen, H.2    Schröder, H.3    McCarty, J.S.4    Virgallita, G.5    Milkereit, P.6    Reinstein, J.7    Bukau, B.8
  • 2
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 & co. - A holding for folding
    • Buchner, J. 1999. Hsp90 & co. - a holding for folding. Trends Biochem. Sci. 24: 136-141.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 136-141
    • Buchner, J.1
  • 3
    • 0031943566 scopus 로고    scopus 로고
    • Analysis of chaperone function using citrate synthase as nonnative substrate protein
    • Buchner, J., Grallert, H., and Jakob, U. 1998. Analysis of chaperone function using citrate synthase as nonnative substrate protein. Methods Enzymol. 290: 323-338.
    • (1998) Methods Enzymol. , vol.290 , pp. 323-338
    • Buchner, J.1    Grallert, H.2    Jakob, U.3
  • 4
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review
    • Csermely, P., Schnaider, T., Söti, C., Prohaszka, Z., and Nardai, G. 1998. The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 79: 129-168.
    • (1998) Pharmacol. Ther. , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Söti, C.3    Prohaszka, Z.4    Nardai, G.5
  • 5
    • 0027513995 scopus 로고
    • The TyrR protein of Escherichia coli: Analysis by limited proteolysis of domain structure and ligand-mediated conformational changes
    • Cui, J., and Somerville, R.L. 1993. The TyrR protein of Escherichia coli: analysis by limited proteolysis of domain structure and ligand-mediated conformational changes. J. Biol. Chem. 268: 5040-5047.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5040-5047
    • Cui, J.1    Somerville, R.L.2
  • 7
    • 0031050734 scopus 로고    scopus 로고
    • Dynamic light scattering in evaluating the crystallizability of macromolecules
    • Ferré-D'Amaré, R., and Burley, S.K. 1997. Dynamic light scattering in evaluating the crystallizability of macromolecules. Methods Enzymol. 276: 157-166.
    • (1997) Methods Enzymol. , vol.276 , pp. 157-166
    • Ferré-D'Amaré, R.1    Burley, S.K.2
  • 8
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty, F.M., DuLuca-Flaherty, C., and McKay, D.B. 1990. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature (London), 346: 623-628.
    • (1990) Nature (London) , vol.346 , pp. 623-628
    • Flaherty, F.M.1    Duluca-Flaherty, C.2    McKay, D.B.3
  • 9
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interactions with HDJ-1
    • Freeman, B.C., Myers, M.P., Schumacher, T., and Morimoto, R.I. 1995. Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interactions with HDJ-1. EMBO (Eur. Mol. Biol. Organ.) J. 14: 2281-2292.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 2281-2292
    • Freeman, B.C.1    Myers, M.P.2    Schumacher, T.3    Morimoto, R.I.4
  • 10
    • 0030834253 scopus 로고    scopus 로고
    • Heat shock protein 80 of Neurospora crassa, a cytosolic molecular chaperone of the eukaryotic stress-90 family, interacts directly with heat shock protein 70
    • Freitag, D.G., Ouimet, P.M., Grivitz, T.L., and Kapoor, M. 1997. Heat shock protein 80 of Neurospora crassa, a cytosolic molecular chaperone of the eukaryotic stress-90 family, interacts directly with heat shock protein 70. Biochemistry, 36: 10 221 -10 229.
    • (1997) Biochemistry , vol.36 , pp. 10221-10229
    • Freitag, D.G.1    Ouimet, P.M.2    Grivitz, T.L.3    Kapoor, M.4
  • 11
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman, J. 2001. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70: 603-647.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 12
    • 0029787852 scopus 로고    scopus 로고
    • Conformations of the nucleotide and polypeptide binding domains of a cytosolic Hsp70 molecular chaperone are coupled
    • Fung, K.L., Hilgenberg, L., Wang, N.M., and Chirico, W.J. 1996. Conformations of the nucleotide and polypeptide binding domains of a cytosolic Hsp70 molecular chaperone are coupled. J. Biol. Chem. 271: 21 559 - 21 565.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21559-21565
    • Fung, K.L.1    Hilgenberg, L.2    Wang, N.M.3    Chirico, W.J.4
  • 13
    • 0029953178 scopus 로고    scopus 로고
    • Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate
    • Gao, B., Eisenberg, E., and Greene, L. 1996. Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate. J. Biol. Chem. 271: 16 792 - 16 797.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16792-16797
    • Gao, B.1    Eisenberg, E.2    Greene, L.3
  • 14
    • 0033673602 scopus 로고    scopus 로고
    • Heat shock protein 80 of Neurospora crassa: Sequence analysis of the gene and expression during the asexual phase
    • Girvitz, T.L., Ouimet, P.M., and Kapoor, M. 2000. Heat shock protein 80 of Neurospora crassa: sequence analysis of the gene and expression during the asexual phase. Can. J. Microbiol. 46: 981-991.
    • (2000) Can. J. Microbiol. , vol.46 , pp. 981-991
    • Girvitz, T.L.1    Ouimet, P.M.2    Kapoor, M.3
  • 15
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. 1996. Molecular chaperones in cellular protein folding. Nature (London), 381: 571-580.
    • (1996) Nature (London) , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 16
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendricks, J.P., and Hartl, F.U. 1993. Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62: 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendricks, J.P.1    Hartl, F.U.2
  • 17
    • 0028940309 scopus 로고
    • Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo
    • Jakob, U., Lilie, H., Meyer, I., and Buchner, J. 1995. Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo. J. Biol. Chem. 270: 7288-7294.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7288-7294
    • Jakob, U.1    Lilie, H.2    Meyer, I.3    Buchner, J.4
  • 19
    • 0142233989 scopus 로고
    • Alteration of protein synthesis pattern in Neurospora crassa cells by hyperthermal and oxidative stress
    • Kapoor, M., and Lewis, J. 1987. Alteration of protein synthesis pattern in Neurospora crassa cells by hyperthermal and oxidative stress. Can. J. Biochem. 55: 43-49.
    • (1987) Can. J. Biochem. , vol.55 , pp. 43-49
    • Kapoor, M.1    Lewis, J.2
  • 20
    • 0028816665 scopus 로고
    • The hsp70 gene family of Neurospora crassa: Cloning, sequence analysis, expression, and genetic mapping of the major stress-inducible member
    • Kapoor, M., Curle, C.A., and Runham, C. 1995. The hsp70 gene family of Neurospora crassa: cloning, sequence analysis, expression, and genetic mapping of the major stress-inducible member. J. Bacteriol. 177: 212-221.
    • (1995) J. Bacteriol. , vol.177 , pp. 212-221
    • Kapoor, M.1    Curle, C.A.2    Runham, C.3
  • 21
    • 14744271625 scopus 로고
    • Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation
    • Kiefhaber, R., Rudolph, H., Kohler, H., and Buchner, J. 1993. Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Bio/Technology, 9: 825.
    • (1993) Bio/Technology , vol.9 , pp. 825
    • Kiefhaber, R.1    Rudolph, H.2    Kohler, H.3    Buchner, J.4
  • 22
    • 0029118986 scopus 로고
    • Polymerization of 70-kDa heat shock protein by yeast DnaJ in ATP
    • King, C., Eisenberg, E., and Greene, L. 1995. Polymerization of 70-kDa heat shock protein by yeast DnaJ in ATP. J. Biol. Chem. 270: 22 535 - 22 540.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22535-22540
    • King, C.1    Eisenberg, E.2    Greene, L.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (London), 227: 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0027916175 scopus 로고
    • Biospecific interaction analysis using biosensor technology
    • Malmqvist, M. 1993. Biospecific interaction analysis using biosensor technology. Nature (London), 361: 186-187.
    • (1993) Nature (London) , vol.361 , pp. 186-187
    • Malmqvist, M.1
  • 26
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
    • Marcu, M.G., Chadli, A., Bouhouche, I., Catelli, M., and Neckers, L.M. 2000. The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J. Biol. Chem. 275: 37 181 - 37 186.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5
  • 28
    • 0033570053 scopus 로고    scopus 로고
    • ATP and the core "α-crystallin" domain of the small heat shock protein αB-crystallin
    • Muchowski, P.J., Hays, L.G., Yates, J.R., III, and Clark, J.I. 1999. ATP and the core "α-crystallin" domain of the small heat shock protein αB-crystallin. J. Biol. Chem. 274: 30 190 - 30 195.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30190-30195
    • Muchowski, P.J.1    Hays, L.G.2    Yates J.R. III3    Clark, J.I.4
  • 29
    • 0033119556 scopus 로고    scopus 로고
    • Instrumental biosensors: New perspectives for the analysis of biomolecular interactions
    • Nice, E.C., and Catimel, M. 1999. Instrumental biosensors: new perspectives for the analysis of biomolecular interactions. Bioessays, 21: 339-352.
    • (1999) Bioessays , vol.21 , pp. 339-352
    • Nice, E.C.1    Catimel, M.2
  • 30
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signaling pathways: Molecular chaperones as stress-sensing "heat shock" proteins
    • Nollen, E.A.A., and Morimoto, R.I. 2002. Chaperoning signaling pathways: molecular chaperones as stress-sensing "heat shock" proteins. J. Cell Sci. 115: 2809-2816.
    • (2002) J. Cell Sci. , vol.115 , pp. 2809-2816
    • Nollen, E.A.A.1    Morimoto, R.I.2
  • 31
    • 0032459050 scopus 로고    scopus 로고
    • Analysis of complex formation between Hsp80 and Hsp70, cytosolic molecular chaperones of Neurospora crassa, by enzyme-linked immunosorbent assays (ELISA)
    • Ouimet, P.M., and Kapoor, M. 1998. Analysis of complex formation between Hsp80 and Hsp70, cytosolic molecular chaperones of Neurospora crassa, by enzyme-linked immunosorbent assays (ELISA). Biochem. Cell Biol. 76: 97-106.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 97-106
    • Ouimet, P.M.1    Kapoor, M.2
  • 32
    • 0032841126 scopus 로고    scopus 로고
    • Nucleotide binding and hydrolysis properties of Neurospora crassa cytosolic molecular chaperones, Hsp70 and Hsp80, heat inducible members of the eukaryotic stress-70 and stress-90 families
    • Ouimet, P.M., and Kapoor, M. 1999. Nucleotide binding and hydrolysis properties of Neurospora crassa cytosolic molecular chaperones, Hsp70 and Hsp80, heat inducible members of the eukaryotic stress-70 and stress-90 families. Biochem. Cell Biol. 77: 89-99.
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 89-99
    • Ouimet, P.M.1    Kapoor, M.2
  • 33
    • 0029889955 scopus 로고    scopus 로고
    • A model of protein targeting mediated by immunophilins and other proteins that bind HSP90 via tetratricopeptide repeat domains
    • Owens-Grillo, J.K., Czar, M.J., Hutchinson, K.A., Hoffmann, K., Perdew, G.K., and Pratt, W.B. 1996. A model of protein targeting mediated by immunophilins and other proteins that bind HSP90 via tetratricopeptide repeat domains. J. Biol. Chem. 271: 13 468 - 13 475.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13468-13475
    • Owens-Grillo, J.K.1    Czar, M.J.2    Hutchinson, K.A.3    Hoffmann, K.4    Perdew, G.K.5    Pratt, W.B.6
  • 35
    • 0004274707 scopus 로고
    • Pharmacia Biosensor AB, Uppsala, Sweden
    • Pharmacia. 1994. BIAtechnology handbook. Pharmacia Biosensor AB, Uppsala, Sweden, pp. 1.2-2.4.
    • (1994) BIAtechnology Handbook , pp. 12-24
  • 36
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou, C., Roe, S.M., O'Brien, R., Ladbury, J.E., Piper, P.W., and Pearl, L.H. 1997. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell, 90: 65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 37
    • 0031106824 scopus 로고    scopus 로고
    • Molecular chaperones: Towards a characterization of the heat-shock protein 70 family
    • Rassow, J., von Ashen, O., Bomer, U., and Pfanner, N. 1997. Molecular chaperones: towards a characterization of the heat-shock protein 70 family. Trends Cell Biol. 7: 129-133.
    • (1997) Trends Cell Biol. , vol.7 , pp. 129-133
    • Rassow, J.1    Von Ashen, O.2    Bomer, U.3    Pfanner, N.4
  • 38
    • 0023957057 scopus 로고
    • Ethanol and carbon-source starvation enhance accumulation of HSP80 in Neurospora crassa
    • Roychowdhury, H.S., and Kapoor, M. 1988. Ethanol and carbon-source starvation enhance accumulation of HSP80 in Neurospora crassa. Can. J. Microbiol. 34: 162-168.
    • (1988) Can. J. Microbiol. , vol.34 , pp. 162-168
    • Roychowdhury, H.S.1    Kapoor, M.2
  • 39
    • 0032539709 scopus 로고    scopus 로고
    • Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence
    • Scheibel, T., Weikl, T., and Buchner, J. 1998. Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. Proc. Natl. Acad. Sci. U.S.A. 95: 1495-1499.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 1495-1499
    • Scheibel, T.1    Weikl, T.2    Buchner, J.3
  • 40
    • 0036263966 scopus 로고    scopus 로고
    • The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase
    • Schiene-Fisher, C., Habazetti, J., Schmid, F.X., and Fisher, G. 2002. The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase. Nature Struct. Biol. 9: 419-424.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 419-424
    • Schiene-Fisher, C.1    Habazetti, J.2    Schmid, F.X.3    Fisher, G.4
  • 41
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Washington, D.C.
    • Schmid, D., Baici, A., Gething, H., and Christen, P. 1994. Kinetics of molecular chaperone action. Science (Washington, D.C.), 263: 971-973.
    • (1994) Science , vol.263 , pp. 971-973
    • Schmid, D.1    Baici, A.2    Gething, H.3    Christen, P.4
  • 42
    • 0028929052 scopus 로고
    • The DnaK chaperone system of Escherichia coli: Quaternary structures and interactions of DnaK and GrpE components
    • Schonfeld, H.-J., Schmidt, D., Schroder, H., and Bukau, B. 1995. The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of DnaK and GrpE components. J. Biol. Chem. 270: 2183-2189.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2183-2189
    • Schonfeld, H.-J.1    Schmidt, D.2    Schroder, H.3    Bukau, B.4
  • 43
    • 0027427986 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schroder, H., Langer, T., Hartl, F.U., and Bakau, B. 1993. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO (Eur. Mol. Biol. Organ.) J. 12: 4137-4144.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 4137-4144
    • Schroder, H.1    Langer, T.2    Hartl, F.U.3    Bakau, B.4
  • 44
    • 0030795295 scopus 로고    scopus 로고
    • Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors
    • Schuck, P. 1997. Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors. Curr. Opin. Biotechnol. 8: 498-502.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 498-502
    • Schuck, P.1
  • 45
    • 0036510547 scopus 로고    scopus 로고
    • A nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90: N-terminal nucleotide binding unmasks a C-terminal pocket
    • Söti, C., Rácz, A., and Csermely, P. 2002. A nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90: N-terminal nucleotide binding unmasks a C-terminal pocket. J. Biol. Chem. 277: 7066-7075.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7066-7075
    • Söti, C.1    Rácz, A.2    Csermely, P.3
  • 46
    • 0024554231 scopus 로고
    • Purification and properties of the Escherichia coli heat shock protein, HtpG
    • Spence, J., and Georgopoulos, C. 1989. Purification and properties of the Escherichia coli heat shock protein, HtpG. J. Biol. Chem. 264: 4396-4402.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4396-4402
    • Spence, J.1    Georgopoulos, C.2
  • 48
    • 0009482260 scopus 로고
    • Electrophoresis transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordan, J. 1979. Electrophoresis transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76: 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordan, J.3
  • 49
    • 0029094250 scopus 로고
    • Divergent effects of ATP on the binding of DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates
    • Wawrzynow, A., and Zylicz, M. 1995. Divergent effects of ATP on the binding of DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates. J. Biol. Chem. 270: 19 300 - 19 306.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19300-19306
    • Wawrzynow, A.1    Zylicz, M.2
  • 52
    • 0021137114 scopus 로고
    • Purification and properties of Escherichia coli DnaK replication protein
    • Zylicz, M., and Georgopoulos, C. 1984. Purification and properties of Escherichia coli DnaK replication protein. J. Biol. Chem. 259: 8820-8825.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8820-8825
    • Zylicz, M.1    Georgopoulos, C.2


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