메뉴 건너뛰기




Volumn 379, Issue 3, 1998, Pages 261-268

Hsp70 chaperone systems: Diversity of cellular functions and mechanism of action

Author keywords

ATPase cycle; DnaJ; DnaK; Protein folding; Stress response

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; HEAT SHOCK PROTEIN 70; PROTEIN; PROTEIN DNAK;

EID: 0031925150     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (137)

References (72)
  • 1
    • 0027067071 scopus 로고
    • Genetics and enzymology of DNA replication in Escherichia coli
    • Baker, T.A., and Wickner, S.H. (1992). Genetics and enzymology of DNA replication in Escherichia coli. Annu. Rev. Genet. 26, 447-477.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 447-477
    • Baker, T.A.1    Wickner, S.H.2
  • 2
    • 0030986955 scopus 로고    scopus 로고
    • Auxilin-induced interaction of the molecular chaperone Hsc70 with clathrin baskets
    • Barouch, W., Prasad, K., Greene, L., and Eisenberg, E. (1997). Auxilin-induced interaction of the molecular chaperone Hsc70 with clathrin baskets. Biochemistry 36, 4303-4308.
    • (1997) Biochemistry , vol.36 , pp. 4303-4308
    • Barouch, W.1    Prasad, K.2    Greene, L.3    Eisenberg, E.4
  • 3
    • 0002830140 scopus 로고
    • Modulation of steroid receptor signal transduction by heat shock proteins
    • R.I. Morimoto, A. Tissières, and C. Georgopoulos, eds. (Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press)
    • Bohen, S.P., and Yamamoto, K.R. (1994). Modulation of steroid receptor signal transduction by heat shock proteins. In: The Biology of Heat Shock Proteins and Molecular Chaperones. R.I. Morimoto, A. Tissières, and C. Georgopoulos, eds. (Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press), pp. 313-334.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 313-334
    • Bohen, S.P.1    Yamamoto, K.R.2
  • 4
    • 0026586906 scopus 로고
    • A module of the DnaJ heat shock proteins found in malaria parasites
    • Bork, P., Sander, C., Valencia, A., and Bukau, B. (1992). A module of the DnaJ heat shock proteins found in malaria parasites. Trends Biochem. Sci. 17, 129.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 129
    • Bork, P.1    Sander, C.2    Valencia, A.3    Bukau, B.4
  • 5
    • 0028879136 scopus 로고
    • Cysteine string protein, a DnaJ family member, is present on diverse secretory vesicles
    • Braun, J.E., and Scheller, R.H. (1995). Cysteine string protein, a DnaJ family member, is present on diverse secretory vesicles. Neuropharmacology 34, 1361-1369.
    • (1995) Neuropharmacology , vol.34 , pp. 1361-1369
    • Braun, J.E.1    Scheller, R.H.2
  • 6
    • 0029911522 scopus 로고    scopus 로고
    • The cysteine string secretory vesicle protein activates Hsc70 ATPase
    • Braun, J.E.A., Wilbanks, S.M., and Scheller, R.H. (1996). The cysteine string secretory vesicle protein activates Hsc70 ATPase. J. Biol. Chem. 271, 25989-25993.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25989-25993
    • Braun, J.E.A.1    Wilbanks, S.M.2    Scheller, R.H.3
  • 7
    • 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, 16903-16910.
    • (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
  • 8
    • 0030598919 scopus 로고    scopus 로고
    • Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding
    • Buchberger, A., Schröder, H., Hesterkamp, T., Schönfeld, H.J., and Bukau, B. (1996). Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J. Mol. Biol. 261, 328-333.
    • (1996) J. Mol. Biol. , vol.261 , pp. 328-333
    • Buchberger, A.1    Schröder, H.2    Hesterkamp, T.3    Schönfeld, H.J.4    Bukau, B.5
  • 9
    • 0031149356 scopus 로고    scopus 로고
    • The DnaJ-like cysteine string protein and exocytotic neurotransmitter release
    • Buchner, E., and Gundersen, C.B. (1997). The DnaJ-like cysteine string protein and exocytotic neurotransmitter release. Trends Neurosci. 20, 223-227.
    • (1997) Trends Neurosci. , vol.20 , pp. 223-227
    • Buchner, E.1    Gundersen, C.B.2
  • 10
    • 0027319272 scopus 로고
    • Regulation of the Escherichia coli heat-shock response
    • Bukau, B. (1993). Regulation of the Escherichia coli heat-shock response. Mol. Microbiol. 9, 671-680.
    • (1993) Mol. Microbiol. , vol.9 , pp. 671-680
    • Bukau, B.1
  • 11
    • 0030560763 scopus 로고    scopus 로고
    • Growing up in a dangerous environment: A network of multiple targeting and folding pathways for nascent polypeptides in the cytosol
    • Bukau, B., Hesterkamp, H., and Luirink, J. (1996). Growing up in a dangerous environment: a network of multiple targeting and folding pathways for nascent polypeptides in the cytosol. Trends Cell Biol. 6, 480-486.
    • (1996) Trends Cell Biol. , vol.6 , pp. 480-486
    • Bukau, B.1    Hesterkamp, H.2    Luirink, J.3
  • 12
    • 0030991023 scopus 로고    scopus 로고
    • Activation of the ATPase activity of heat-shock proteins Hsc70/Hsp70 by cysteine-string protein
    • Chamberlain, L.H., and Burgoyne, R.D. (1997). Activation of the ATPase activity of heat-shock proteins Hsc70/Hsp70 by cysteine-string protein. Biochem. J. 322, 853-858.
    • (1997) Biochem. J. , vol.322 , pp. 853-858
    • Chamberlain, L.H.1    Burgoyne, R.D.2
  • 14
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein synthesis
    • Craig, E.A., Gambill, B.D., and Nelson, R.J. (1993). Heat shock proteins: molecular chaperones of protein synthesis. Microbiological Reviews 57, 402-414.
    • (1993) Microbiological Reviews , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 15
    • 0002237472 scopus 로고
    • Cytosolic hsp70s of Saccharomyces cerevisiae: Roles in protein synthesis, protein translocation, proteolysis, and regulation
    • R.I. Morimoto, A. Tissières, and C. Georgopoulos, eds., (Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press)
    • Craig, E.A., Baxter, B.K., Becker, J., Halladay, J., and Ziegelhoffer, T. (1994). Cytosolic hsp70s of Saccharomyces cerevisiae: Roles in protein synthesis, protein translocation, proteolysis, and regulation. In: The Biology of Heat Shock Proteins and Molecular Chaperones. R.I. Morimoto, A. Tissières, and C. Georgopoulos, eds., (Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press), pp. 31-52.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 31-52
    • Craig, E.A.1    Baxter, B.K.2    Becker, J.3    Halladay, J.4    Ziegelhoffer, T.5
  • 16
    • 0344470984 scopus 로고
    • Differential regulation of Hsp70 subfamilies by the eukaryotic DnaJ homologue YDJ1
    • Cyr, D.M., and Douglas, M.G. (1994). Differential regulation of Hsp70 subfamilies by the eukaryotic DnaJ homologue YDJ1. Proc. Natl. Acad. Sci. USA 91, 2066-2070.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2066-2070
    • Cyr, D.M.1    Douglas, M.G.2
  • 17
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty, K.M., DeLuca-Flaherty, C., and McKay, D.B. (1990). Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346, 623-628.
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 18
    • 0025753142 scopus 로고
    • Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein
    • Flaherty, K.M., McKay, D.B., Kabsch, W., and Holmes, K.C. (1991). Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc. Natl. Acad. Sci. USA 88, 5041-5045.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5041-5045
    • Flaherty, K.M.1    McKay, D.B.2    Kabsch, W.3    Holmes, K.C.4
  • 19
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn, G.C., Pohl, J., Flocco, M.T., and Rothman, J.E. (1991). Peptide-binding specificity of the molecular chaperone BiP. Nature 353, 726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 20
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman, J., and Höhfeld, J. (1997). Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci. 22, 87-92.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Höhfeld, J.2
  • 21
    • 0030044799 scopus 로고    scopus 로고
    • A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32
    • Gamer, J., Multhaup, G., Tomoyasu, T., McCarty, J.S., Rüdiger, S., Schönfeld, H.J., Schirra, C., Bujard, H., and Bukau, B. (1996). A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J. 15, 607-617.
    • (1996) EMBO J. , vol.15 , pp. 607-617
    • Gamer, J.1    Multhaup, G.2    Tomoyasu, T.3    McCarty, J.S.4    Rüdiger, S.5    Schönfeld, H.J.6    Schirra, C.7    Bujard, H.8    Bukau, B.9
  • 22
    • 0030671388 scopus 로고    scopus 로고
    • Proteins interacting with the molecular chaperone hsp70/hsc70: Physical associations and effects on refolding activity
    • Gebauer, M., Zeiner, M., and Gehring, U. (1997). Proteins interacting with the molecular chaperone hsp70/hsc70: physical associations and effects on refolding activity. FEBS Lett. 417, 109-113.
    • (1997) FEBS Lett. , vol.417 , pp. 109-113
    • Gebauer, M.1    Zeiner, M.2    Gehring, U.3
  • 23
    • 0001241680 scopus 로고    scopus 로고
    • Function and regulation of the heat shock proteins
    • F.C. Neidhardt, ed., (Washington: ASM Press)
    • Gross, C.A. (1996). Function and regulation of the heat shock proteins. In: Escherichia coli and Salmonella. F.C. Neidhardt, ed., (Washington: ASM Press), pp. 1382-1399.
    • (1996) Escherichia Coli and Salmonella , pp. 1382-1399
    • Gross, C.A.1
  • 24
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison, C.J., Hayer-Hartl, M., Di Liberto, M., Hartl, F., and Kuriyan, J. (1997). Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276, 431-435.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.4    Kuriyan, J.5
  • 25
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 26
    • 0030052910 scopus 로고    scopus 로고
    • Roles of molecular chaperones in protein degradation
    • Hayes, S.A., and Dice, J.F. (1996). Roles of molecular chaperones in protein degradation. J. Cell Biol. 132, 255-258.
    • (1996) J. Cell Biol. , vol.132 , pp. 255-258
    • Hayes, S.A.1    Dice, J.F.2
  • 27
    • 0029651968 scopus 로고
    • 1H and 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78)
    • Hill, R.B., Flanagan, J.M., and Prestegard, J.H. (1995). 1H and 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78). Biochemistry 34, 5587-5596.
    • (1995) Biochemistry , vol.34 , pp. 5587-5596
    • Hill, R.B.1    Flanagan, J.M.2    Prestegard, J.H.3
  • 28
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Höhfeld, J., Minami, Y., and Hartl, F.U. (1995). Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83, 589-598.
    • (1995) Cell , vol.83 , pp. 589-598
    • Höhfeld, J.1    Minami, Y.2    Hartl, F.U.3
  • 29
    • 0344039806 scopus 로고    scopus 로고
    • GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1
    • Höhfeld, J., and Jentsch, S. (1997). GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16, 6209-6216.
    • (1997) EMBO J. , vol.16 , pp. 6209-6216
    • Höhfeld, J.1    Jentsch, S.2
  • 30
    • 0029846829 scopus 로고    scopus 로고
    • Mechanism of clathrin basket dissociation: Separate functions of protein domains of the DnaJ homologue auxilin
    • Holstein, S.E., Ungewickell, H., and Ungewickell, E. (1996). Mechanism of clathrin basket dissociation: separate functions of protein domains of the DnaJ homologue auxilin. J. Cell Biol. 135, 925-937.
    • (1996) J. Cell Biol. , vol.135 , pp. 925-937
    • Holstein, S.E.1    Ungewickell, H.2    Ungewickell, E.3
  • 31
    • 15844372190 scopus 로고    scopus 로고
    • A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
    • Karzai, A.W., and McMacken, R. (1996). A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J. Biol. Chem. 271, 11236-11246.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11236-11246
    • Karzai, A.W.1    McMacken, R.2
  • 32
    • 0028300711 scopus 로고
    • Chaperone power in a virus? Trends Biochem
    • Kelley, W.L., and Landry, S.J. (1994). Chaperone power in a virus? Trends Biochem. Sci. 19, 277-278.
    • (1994) Sci. , vol.19 , pp. 277-278
    • Kelley, W.L.1    Landry, S.J.2
  • 33
    • 0030883403 scopus 로고    scopus 로고
    • Positive control of the two-component RcsC/B signal transduction network by DjIA: A member of the DnaJ family of molecular chaperones in Escherichia coli
    • Kelley, W.L., and Georgopoulos, C. (1997a). Positive control of the two-component RcsC/B signal transduction network by DjIA: a member of the DnaJ family of molecular chaperones in Escherichia coli. Mol. Microbiol. 25, 913-931.
    • (1997) Mol. Microbiol. , vol.25 , pp. 913-931
    • Kelley, W.L.1    Georgopoulos, C.2
  • 34
    • 0030935256 scopus 로고    scopus 로고
    • The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperone
    • Kelley, W.L., and Georgopoulos, C. (1997b). The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperone. Proc. Natl. Acad. Sci. USA 94, 3679-3684.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3679-3684
    • Kelley, W.L.1    Georgopoulos, C.2
  • 35
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M.K., and Hartl, F.U. (1992). Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356, 683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 37
    • 0026320296 scopus 로고
    • The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein
    • Liberek, K., Skowyra, D., Zylicz, M., Johnson, C., and Georgopoulos, C. (1991). The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein. J. Biol. Chem. 266, 14491-14496.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14491-14496
    • Liberek, K.1    Skowyra, D.2    Zylicz, M.3    Johnson, C.4    Georgopoulos, C.5
  • 38
    • 0029052538 scopus 로고
    • The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator
    • Liberek, K., Wall, D., and Georgopoulos, C. (1995). The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator. Proc. Natl. Acad. Sci. USA 92, 6224-6228.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6224-6228
    • Liberek, K.1    Wall, D.2    Georgopoulos, C.3
  • 39
    • 0030469215 scopus 로고    scopus 로고
    • Polypeptide translocation machinery of the yeast endoplasmic reticulum
    • Lyman, S.K., and Schekman, R. (1996). Polypeptide translocation machinery of the yeast endoplasmic reticulum. Experientia 52, 1042-1049.
    • (1996) Experientia , vol.52 , pp. 1042-1049
    • Lyman, S.K.1    Schekman, R.2
  • 40
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty, J.S., Buchberger, A., Reinstein, J., and Bukau, B. (1995). The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249, 126-137.
    • (1995) J. Mol. Biol. , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 41
    • 0029683566 scopus 로고    scopus 로고
    • The transcriptional regulation of heat shock genes: A plethora of heat shock factors and regulatory conditions
    • U. Feige, R.I. Morimoto, I. Yahara, and B.S. Polla, eds., (Basel, Switzerland: Birkhäuser Verlag)
    • Morimoto, R.I., Kroeger, P.E., and Cotto, J.J. (1996). The transcriptional regulation of heat shock genes: A plethora of heat shock factors and regulatory conditions. In: Stress-Inducible Cellular Responses. U. Feige, R.I. Morimoto, I. Yahara, and B.S. Polla, eds., (Basel, Switzerland: Birkhäuser Verlag), pp. 139-163.
    • (1996) Stress-Inducible Cellular Responses , pp. 139-163
    • Morimoto, R.I.1    Kroeger, P.E.2    Cotto, J.J.3
  • 42
    • 0029825801 scopus 로고    scopus 로고
    • DnaK heat shock protein of Escherichia coli maintains the negative supercoiling of DNA against thermal stress
    • Ogata, Y., Mizushima, T., Kataoka, K., Kita, K., Miki, T., and Sekimizu, K. (1996). DnaK heat shock protein of Escherichia coli maintains the negative supercoiling of DNA against thermal stress. J. Biol. Chem. 271, 29407-29414.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29407-29414
    • Ogata, Y.1    Mizushima, T.2    Kataoka, K.3    Kita, K.4    Miki, T.5    Sekimizu, K.6
  • 43
    • 0030945296 scopus 로고    scopus 로고
    • GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism
    • Packschies, L., Theyssen, H., Buchberger, A., Bukau, B., Goody, R.S., and Reinstein, J. (1997). GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry 36, 3417-3422.
    • (1997) Biochemistry , vol.36 , pp. 3417-3422
    • Packschies, L.1    Theyssen, H.2    Buchberger, A.3    Bukau, B.4    Goody, R.S.5    Reinstein, J.6
  • 44
    • 0027322906 scopus 로고
    • Three-state denaturation of DnaK induced by guanidine hydrochloride. Evidence for an expandable intermediate
    • Palleros, D.R., Shi, L., Reid, K.L., and Fink, A.L. (1993). Three-state denaturation of DnaK induced by guanidine hydrochloride. Evidence for an expandable intermediate. Biochemistry 32, 4314-4321.
    • (1993) Biochemistry , vol.32 , pp. 4314-4321
    • Palleros, D.R.1    Shi, L.2    Reid, K.L.3    Fink, A.L.4
  • 45
    • 0030581175 scopus 로고    scopus 로고
    • NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone
    • Pellecchia, M., Szyperski, T., Wall, D., Georgopoulos, C., and Wuthrich, K. (1996). NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. J. Mol. Biol. 260, 236-250.
    • (1996) J. Mol. Biol. , vol.260 , pp. 236-250
    • Pellecchia, M.1    Szyperski, T.2    Wall, D.3    Georgopoulos, C.4    Wuthrich, K.5
  • 48
    • 0030581148 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain
    • Qian, Y.Q., Patel, D., Haiti, F.U., and McColl, D.J. (1996). Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. J. Mol. Biol. 260, 224-235.
    • (1996) J. Mol. Biol. , vol.260 , pp. 224-235
    • Qian, Y.Q.1    Patel, D.2    Haiti, F.U.3    McColl, D.J.4
  • 49
    • 0023041382 scopus 로고
    • Enzymatic recycling of clathrin from coated vesicles
    • Rothman, J.E., and Schmid, S.L. (1986). Enzymatic recycling of clathrin from coated vesicles. Cell 46, 5-9.
    • (1986) Cell , vol.46 , pp. 5-9
    • Rothman, J.E.1    Schmid, S.L.2
  • 50
    • 0041026092 scopus 로고    scopus 로고
    • Interaction of Hsp70 chaperones with substrates
    • Rüdiger, S., Buchberger, A., and Bukau, B. (1997). Interaction of Hsp70 chaperones with substrates. Nat. Struct. Biol. 4, 342-349.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 342-349
    • Rüdiger, S.1    Buchberger, A.2    Bukau, B.3
  • 51
    • 0032512425 scopus 로고    scopus 로고
    • Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone
    • Russell, R., Jordan, R., and McMacken, R. (1998). Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone. Biochemistry 37, 596-607.
    • (1998) Biochemistry , vol.37 , pp. 596-607
    • Russell, R.1    Jordan, R.2    McMacken, R.3
  • 52
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and Dobberstein, B. (1996). Common principles of protein translocation across membranes. Science 271, 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 53
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid, D., Baici, A., Gehring, H., and Christen, P. (1994). Kinetics of molecular chaperone action. Science 263, 971-973.
    • (1994) Science , vol.263 , pp. 971-973
    • Schmid, D.1    Baici, A.2    Gehring, H.3    Christen, P.4
  • 54
    • 26744442851 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schröder, H., Langer, T., Hartl, F.U., and Bukau, B. (1993). DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. FEMS Microbiol. Lett. 113, 93-99.
    • (1993) FEMS Microbiol. Lett. , vol.113 , pp. 93-99
    • Schröder, H.1    Langer, T.2    Hartl, F.U.3    Bukau, B.4
  • 55
    • 0029684296 scopus 로고    scopus 로고
    • Involvement of molecular chaperones in intracellular protein breakdown
    • Sherman, M.Y., and Goldberg, A.L. (1996). Involvement of molecular chaperones in intracellular protein breakdown. Exs 77, 57-78.
    • (1996) Exs , vol.77 , pp. 57-78
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 56
    • 0029876864 scopus 로고    scopus 로고
    • Conformational characterization of DnaK and its complexes by small- Angle X-ray scattering
    • Shi, L., Kataoka, M., and Fink, A.L. (1996). Conformational characterization of DnaK and its complexes by small-angle X-ray scattering. Biochemistry 35, 3297-3308.
    • (1996) Biochemistry , vol.35 , pp. 3297-3308
    • Shi, L.1    Kataoka, M.2    Fink, A.L.3
  • 57
    • 0026707466 scopus 로고
    • DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli
    • Shi, W., Zhou, Y., Wild, J., Adler, J., and Gross, C.A. (1992). DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli. J. Bacteriol.174, 6256-6263.
    • (1992) J. Bacteriol. , vol.174 , pp. 6256-6263
    • Shi, W.1    Zhou, Y.2    Wild, J.3    Adler, J.4    Gross, C.A.5
  • 58
    • 0027169533 scopus 로고
    • Eukaryotic DnaJ homologs and the specificity of Hsp70 activity
    • Silver, P.A., and Way, J.C. (1993). Eukaryotic DnaJ homologs and the specificity of Hsp70 activity. Cell 74, 5-6.
    • (1993) Cell , vol.74 , pp. 5-6
    • Silver, P.A.1    Way, J.C.2
  • 59
    • 0031569356 scopus 로고    scopus 로고
    • Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain
    • Sriram, M., Osipiuk, J., Freeman, B., Morimoto, R., and Joachimiak, A. (1997). Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain. Structure 5, 403-414.
    • (1997) Structure , vol.5 , pp. 403-414
    • Sriram, M.1    Osipiuk, J.2    Freeman, B.3    Morimoto, R.4    Joachimiak, A.5
  • 60
    • 0027958293 scopus 로고
    • Mitochondrial molecular chaperones: Their role in protein translocation
    • Stuart, R.A., Cyr, D.M., Craig, E.A., and Neupert, W. (1994). Mitochondrial molecular chaperones: their role in protein translocation. Trends Biochem. Sci. 19, 87-92.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 87-92
    • Stuart, R.A.1    Cyr, D.M.2    Craig, E.A.3    Neupert, W.4
  • 61
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE
    • Szabo, A., Langer, T., Schröder, H., Flanagan, J., Bukau, B., and Hartl, F.U. (1994). The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. USA 91, 10345-10349.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schröder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, F.U.6
  • 62
    • 0027987996 scopus 로고
    • NMR structure determination of the Escherichia coli DnaJ molecular chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain
    • Szyperski, T., Pellecchia, M., Wall, D., Georgopoulos, C., and Wuthrich, K. (1994). NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain. Proc. Natl. Acad. Sci. USA 91, 11343-11347.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11343-11347
    • Szyperski, T.1    Pellecchia, M.2    Wall, D.3    Georgopoulos, C.4    Wuthrich, K.5
  • 65
    • 0027979545 scopus 로고
    • An analogue of the DnaJ molecular chaperone in Escherichia coli
    • Ueguchi, C., Kakeda, M., Yamada, H., and Mizuno, T. (1994). An analogue of the DnaJ molecular chaperone in Escherichia coli. Proc. Natl. Acad. Sci. USA 91, 1054-1058.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1054-1058
    • Ueguchi, C.1    Kakeda, M.2    Yamada, H.3    Mizuno, T.4
  • 67
    • 0029094250 scopus 로고
    • Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates
    • Wawrzynów, A., and Zylicz, M. (1995). Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates. J. Biol. Chem. 270, 19300-19306.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19300-19306
    • Wawrzynów, A.1    Zylicz, M.2
  • 68
    • 0029842087 scopus 로고    scopus 로고
    • The cbpA chaperone gene function compensates for dnaJ in lambda plasmid replication during amino acid starvation of Escherichia coli
    • Wegrzyn, A., Taylor, K., and Wegrzyn, G. (1996). The cbpA chaperone gene function compensates for dnaJ in lambda plasmid replication during amino acid starvation of Escherichia coli. J. Bacteriol. 178, 5847-5849.
    • (1996) J. Bacteriol. , vol.178 , pp. 5847-5849
    • Wegrzyn, A.1    Taylor, K.2    Wegrzyn, G.3
  • 69
    • 0029893301 scopus 로고    scopus 로고
    • Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli
    • Wild, J., Rossmeissl, P., Walter, W.A., and Gross, C.A. (1996). Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli. J. Bacteriol. 178, 3608-3613.
    • (1996) J. Bacteriol. , vol.178 , pp. 3608-3613
    • Wild, J.1    Rossmeissl, P.2    Walter, W.A.3    Gross, C.A.4
  • 70
    • 0029682521 scopus 로고    scopus 로고
    • Transcriptional regulation of stress-inducible genes in prokaryotes
    • U. Feige, R.I. Morimoto, I. Yahara, and B.S. Polla, eds. (Basel, Switzerland: Birkhäuser Verlag)
    • Yura, T., Nagahigashi, K., and Kanemori, M. (1996). Transcriptional regulation of stress-inducible genes in prokaryotes. In: Stress-Inducible Cellular Responses. U. Feige, R.I. Morimoto, I. Yahara, and B.S. Polla, eds. (Basel, Switzerland: Birkhäuser Verlag), pp. 165-181.
    • (1996) Stress-Inducible Cellular Responses , pp. 165-181
    • Yura, T.1    Nagahigashi, K.2    Kanemori, M.3
  • 71
    • 0030766734 scopus 로고    scopus 로고
    • Mammalian protein RAP46: An interaction partner and modulator of 70 kDa heat shock proteins
    • Zeiner, M., Gebauer, M., and Gehring, U. (1997). Mammalian protein RAP46: an interaction partner and modulator of 70 kDa heat shock proteins. EMBO J. 16, 5483-5490.
    • (1997) EMBO J. , vol.16 , pp. 5483-5490
    • Zeiner, M.1    Gebauer, M.2    Gehring, U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.