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Volumn 425, Issue 3, 2013, Pages 466-474

Conformational selection in substrate recognition by Hsp70 chaperones

Author keywords

antibody; BiP; Hsp70; Keywords; molecular chaperone; substrate conformation

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70;

EID: 84872870534     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.11.030     Document Type: Article
Times cited : (39)

References (46)
  • 1
    • 77955506092 scopus 로고    scopus 로고
    • Gymnastics of molecular chaperones
    • M.P. Mayer Gymnastics of molecular chaperones Mol. Cell 39 2010 321 331
    • (2010) Mol. Cell , vol.39 , pp. 321-331
    • Mayer, M.P.1
  • 2
    • 34547146401 scopus 로고    scopus 로고
    • The mechanism of Hsp70 chaperones: (Entropic) pulling the models together
    • P. Goloubinoff, and P. De Los Rios The mechanism of Hsp70 chaperones: (entropic) pulling the models together Trends Biochem. Sci. 32 2007 372 380
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 372-380
    • Goloubinoff, P.1    De Los Rios, P.2
  • 3
    • 34047268015 scopus 로고    scopus 로고
    • Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker
    • J.F. Swain, G. Dinler, R. Sivendran, D.L. Montgomery, M. Stotz, and L.M. Gierasch Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker Mol. Cell 26 2007 27 39
    • (2007) Mol. Cell , vol.26 , pp. 27-39
    • Swain, J.F.1    Dinler, G.2    Sivendran, R.3    Montgomery, D.L.4    Stotz, M.5    Gierasch, L.M.6
  • 4
    • 0029911568 scopus 로고    scopus 로고
    • Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone
    • S. Takeda, and D.B. McKay Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone Biochemistry 35 1996 4636 4644
    • (1996) Biochemistry , vol.35 , pp. 4636-4644
    • Takeda, S.1    McKay, D.B.2
  • 6
    • 0031764686 scopus 로고    scopus 로고
    • Heat shock protein 70 family: Multiple sequence comparisons, function, and evolution
    • S. Karlin, and L. Brocchieri Heat shock protein 70 family: multiple sequence comparisons, function, and evolution J. Mol. Evol. 47 1998 565 577
    • (1998) J. Mol. Evol. , vol.47 , pp. 565-577
    • Karlin, S.1    Brocchieri, L.2
  • 7
  • 8
    • 0033569993 scopus 로고    scopus 로고
    • BiP-binding sequences in HIV gp160. Implications for the binding specificity of bip
    • G. Knarr, S. Modrow, A. Todd, M.J. Gething, and J. Buchner BiP-binding sequences in HIV gp160. Implications for the binding specificity of bip J. Biol. Chem. 274 1999 29850 29857
    • (1999) J. Biol. Chem. , vol.274 , pp. 29850-29857
    • Knarr, G.1    Modrow, S.2    Todd, A.3    Gething, M.J.4    Buchner, J.5
  • 10
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • S. Rudiger, L. Germeroth, J. Schneider-Mergener, and B. Bukau Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries EMBO J. 16 1997 1501 1507
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rudiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 11
    • 0028085844 scopus 로고
    • Different peptide binding specificities of hsp70 family members
    • A. Gragerov, and M.E. Gottesman Different peptide binding specificities of hsp70 family members J. Mol. Biol. 241 1994 133 135
    • (1994) J. Mol. Biol. , vol.241 , pp. 133-135
    • Gragerov, A.1    Gottesman, M.E.2
  • 12
    • 79952833763 scopus 로고    scopus 로고
    • The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities
    • J. Hageman, M.A. van Waarde, A. Zylicz, D. Walerych, and H.H. Kampinga The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities Biochem. J. 435 2011 127 142
    • (2011) Biochem. J. , vol.435 , pp. 127-142
    • Hageman, J.1    Van Waarde, M.A.2    Zylicz, A.3    Walerych, D.4    Kampinga, H.H.5
  • 13
    • 0027405024 scopus 로고
    • Hsc70, immunoglobulin heavy chain binding protein, and Hsp90 differ in their ability to stimulate transport of precursor proteins into mammalian microsomes
    • H. Wiech, J. Buchner, M. Zimmermann, R. Zimmermann, and U. Jakob Hsc70, immunoglobulin heavy chain binding protein, and Hsp90 differ in their ability to stimulate transport of precursor proteins into mammalian microsomes J. Biol. Chem. 268 1993 7414 7421
    • (1993) J. Biol. Chem. , vol.268 , pp. 7414-7421
    • Wiech, H.1    Buchner, J.2    Zimmermann, M.3    Zimmermann, R.4    Jakob, U.5
  • 15
    • 0042970598 scopus 로고    scopus 로고
    • Dependence of endoplasmic reticulum-Associated degradation on the peptide binding domain and concentration of BiP
    • M. Kabani, S.S. Kelley, M.W. Morrow, D.L. Montgomery, R. Sivendran, and M.D. Rose Dependence of endoplasmic reticulum-Associated degradation on the peptide binding domain and concentration of BiP Mol. Biol. Cell 14 2003 3437 3448
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3437-3448
    • Kabani, M.1    Kelley, S.S.2    Morrow, M.W.3    Montgomery, D.L.4    Sivendran, R.5    Rose, M.D.6
  • 16
    • 0024278557 scopus 로고
    • Heavy-chain binding protein recognizes aberrant polypeptides translocated in vitro
    • C.K. Kassenbrock, P.D. Garcia, P. Walter, and R.B. Kelly Heavy-chain binding protein recognizes aberrant polypeptides translocated in vitro Nature 333 1988 90 93
    • (1988) Nature , vol.333 , pp. 90-93
    • Kassenbrock, C.K.1    Garcia, P.D.2    Walter, P.3    Kelly, R.B.4
  • 17
    • 0033214526 scopus 로고    scopus 로고
    • Mapping the major interaction between binding protein and Ig light chains to sites within the variable domain
    • D.P. Davis, R. Khurana, S. Meredith, F.J. Stevens, and Y. Argon Mapping the major interaction between binding protein and Ig light chains to sites within the variable domain J. Immunol. 163 1999 3842 3850
    • (1999) J. Immunol. , vol.163 , pp. 3842-3850
    • Davis, D.P.1    Khurana, R.2    Meredith, S.3    Stevens, F.J.4    Argon, Y.5
  • 18
    • 0033545187 scopus 로고    scopus 로고
    • The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP
    • R. Hellman, M. Vanhove, A. Lejeune, F.J. Stevens, and L.M. Hendershot The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP J. Cell Biol. 144 1999 21 30
    • (1999) J. Cell Biol. , vol.144 , pp. 21-30
    • Hellman, R.1    Vanhove, M.2    Lejeune, A.3    Stevens, F.J.4    Hendershot, L.M.5
  • 19
    • 34548753384 scopus 로고    scopus 로고
    • Stable interaction of the cargo receptor VIP36 with molecular chaperone BiP
    • D. Nawa, O. Shimada, N. Kawasaki, N. Matsumoto, and K. Yamamoto Stable interaction of the cargo receptor VIP36 with molecular chaperone BiP Glycobiology 17 2007 913 921
    • (2007) Glycobiology , vol.17 , pp. 913-921
    • Nawa, D.1    Shimada, O.2    Kawasaki, N.3    Matsumoto, N.4    Yamamoto, K.5
  • 20
    • 0034896499 scopus 로고    scopus 로고
    • Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release
    • M. Vanhove, Y.K. Usherwood, and L.M. Hendershot Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release Immunity 15 2001 105 114
    • (2001) Immunity , vol.15 , pp. 105-114
    • Vanhove, M.1    Usherwood, Y.K.2    Hendershot, L.M.3
  • 21
    • 0021076098 scopus 로고
    • Immunoglobulin heavy chain binding protein
    • I.G. Haas, and M. Wabl Immunoglobulin heavy chain binding protein Nature 306 1983 387 389
    • (1983) Nature , vol.306 , pp. 387-389
    • Haas, I.G.1    Wabl, M.2
  • 22
    • 0022536233 scopus 로고
    • Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas
    • D.G. Bole, L.M. Hendershot, and J.F. Kearney Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas J. Cell Biol. 102 1986 1558 1566
    • (1986) J. Cell Biol. , vol.102 , pp. 1558-1566
    • Bole, D.G.1    Hendershot, L.M.2    Kearney, J.F.3
  • 23
    • 0025007007 scopus 로고
    • Immunoglobulin heavy chain and binding protein complexes are dissociated in vivo by light chain addition
    • L.M. Hendershot Immunoglobulin heavy chain and binding protein complexes are dissociated in vivo by light chain addition J. Cell Biol. 111 1990 829 837
    • (1990) J. Cell Biol. , vol.111 , pp. 829-837
    • Hendershot, L.M.1
  • 24
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • L. Meunier, Y.K. Usherwood, K.T. Chung, and L.M. Hendershot A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins Mol. Biol. Cell 13 2002 4456 4469
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 26
    • 0032838622 scopus 로고    scopus 로고
    • BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly
    • Y.K. Lee, J.W. Brewer, R. Hellman, and L.M. Hendershot BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly Mol. Biol. Cell 10 1999 2209 2219
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2209-2219
    • Lee, Y.K.1    Brewer, J.W.2    Hellman, R.3    Hendershot, L.M.4
  • 27
    • 0023096246 scopus 로고
    • Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein
    • L. Hendershot, D. Bole, G. Kohler, and J.F. Kearney Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein J. Cell Biol. 104 1987 761 767
    • (1987) J. Cell Biol. , vol.104 , pp. 761-767
    • Hendershot, L.1    Bole, D.2    Kohler, G.3    Kearney, J.F.4
  • 29
    • 0037666981 scopus 로고    scopus 로고
    • Modulation of the ATPase cycle of BiP by peptides and proteins
    • M. Mayer, J. Reinstein, and J. Buchner Modulation of the ATPase cycle of BiP by peptides and proteins J. Mol. Biol. 330 2003 137 144
    • (2003) J. Mol. Biol. , vol.330 , pp. 137-144
    • Mayer, M.1    Reinstein, J.2    Buchner, J.3
  • 31
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • G.C. Flynn, J. Pohl, M.T. Flocco, and J.E. Rothman Peptide-binding specificity of the molecular chaperone BiP Nature 353 1991 726 730
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 32
    • 79551632223 scopus 로고    scopus 로고
    • Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions
    • M. Marcinowski, M. Holler, M.J. Feige, D. Baerend, D.C. Lamb, and J. Buchner Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions Nat. Struct. Mol. Biol. 18 2011 150 158
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 150-158
    • Marcinowski, M.1    Holler, M.2    Feige, M.J.3    Baerend, D.4    Lamb, D.C.5    Buchner, J.6
  • 33
    • 0017152608 scopus 로고
    • Crystallographic structure studies of an IgG molecule and an Fc fragment
    • R. Huber, J. Deisenhofer, P.M. Colman, M. Matsushima, and W. Palm Crystallographic structure studies of an IgG molecule and an Fc fragment Nature 264 1976 415 420
    • (1976) Nature , vol.264 , pp. 415-420
    • Huber, R.1    Deisenhofer, J.2    Colman, P.M.3    Matsushima, M.4    Palm, W.5
  • 34
    • 77951223167 scopus 로고    scopus 로고
    • DynaDock: A new molecular dynamics-based algorithm for protein-peptide docking including receptor flexibility
    • I. Antes DynaDock: a new molecular dynamics-based algorithm for protein-peptide docking including receptor flexibility Proteins 78 2010 1084 1104
    • (2010) Proteins , vol.78 , pp. 1084-1104
    • Antes, I.1
  • 35
    • 0034397884 scopus 로고    scopus 로고
    • Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch
    • S. Rudiger, M.P. Mayer, J. Schneider-Mergener, and B. Bukau Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch J. Mol. Biol. 304 2000 245 251
    • (2000) J. Mol. Biol. , vol.304 , pp. 245-251
    • Rudiger, S.1    Mayer, M.P.2    Schneider-Mergener, J.3    Bukau, B.4
  • 36
    • 62649101873 scopus 로고    scopus 로고
    • Allosteric coupling between the lid and interdomain linker in DnaK revealed by inhibitor binding studies
    • M. Liebscher, and A. Roujeinikova Allosteric coupling between the lid and interdomain linker in DnaK revealed by inhibitor binding studies J. Bacteriol. 191 2009 1456 1462
    • (2009) J. Bacteriol. , vol.191 , pp. 1456-1462
    • Liebscher, M.1    Roujeinikova, A.2
  • 38
    • 79953695041 scopus 로고    scopus 로고
    • Rational design of oncocin derivatives with superior protease stabilities and antibacterial activities based on the high-resolution structure of the oncocin-DnaK complex
    • D. Knappe, M. Zahn, U. Sauer, G. Schiffer, N. Strater, and R. Hoffmann Rational design of oncocin derivatives with superior protease stabilities and antibacterial activities based on the high-resolution structure of the oncocin-DnaK complex Chembiochem 12 2011 874 876
    • (2011) Chembiochem , vol.12 , pp. 874-876
    • Knappe, D.1    Zahn, M.2    Sauer, U.3    Schiffer, G.4    Strater, N.5    Hoffmann, R.6
  • 39
    • 84864148170 scopus 로고    scopus 로고
    • Api88 is a novel antibacterial designer peptide to treat systemic infections with multidrug-resistant gram-negative pathogens
    • P. Czihal, D. Knappe, S. Fritsche, M. Zahn, N. Berthold, and S. Piantavigna Api88 is a novel antibacterial designer peptide to treat systemic infections with multidrug-resistant gram-negative pathogens ACS Chem. Biol. 7 2012 1281 1291
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1281-1291
    • Czihal, P.1    Knappe, D.2    Fritsche, S.3    Zahn, M.4    Berthold, N.5    Piantavigna, S.6
  • 40
    • 0029996090 scopus 로고    scopus 로고
    • Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria
    • J.S. McCarty, S. Rudiger, H.J. Schonfeld, J. Schneider-Mergener, K. Nakahigashi, T. Yura, and B. Bukau Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria J. Mol. Biol. 256 1996 829 837
    • (1996) J. Mol. Biol. , vol.256 , pp. 829-837
    • McCarty, J.S.1    Rudiger, S.2    Schonfeld, H.J.3    Schneider-Mergener, J.4    Nakahigashi, K.5    Yura, T.6    Bukau, B.7
  • 41
    • 0021137114 scopus 로고
    • Purification and properties of the Escherichia coli dnaK replication protein
    • M. Zylicz, and C. Georgopoulos Purification and properties of the Escherichia coli dnaK replication protein J. Biol. Chem. 259 1984 8820 8825
    • (1984) J. Biol. Chem. , vol.259 , pp. 8820-8825
    • Zylicz, M.1    Georgopoulos, C.2
  • 42
    • 0008783803 scopus 로고
    • Solid-phase peptide syntheses
    • R.B. Merrifield Solid-phase peptide syntheses Endeavour 24 1965 3 7
    • (1965) Endeavour , vol.24 , pp. 3-7
    • Merrifield, R.B.1
  • 43
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • M. Schnolzer, P. Alewood, A. Jones, D. Alewood, and S.B. Kent In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences Int. J. Pept. Protein Res. 40 1992 180 193
    • (1992) Int. J. Pept. Protein Res. , vol.40 , pp. 180-193
    • Schnolzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.5
  • 44
    • 2142752826 scopus 로고
    • 9-Fluorenylmethoxycarbonyl function, a new base-sensitive amino-protecting group
    • L.A. Carpino, and G.Y. Han 9-Fluorenylmethoxycarbonyl function, a new base-sensitive amino-protecting group J. Am. Chem. Soc. 92 1970 5748 5749
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 5748-5749
    • Carpino, L.A.1    Han, G.Y.2
  • 45
    • 0141978673 scopus 로고    scopus 로고
    • Comparative protein structure modeling by iterative alignment, model building and model assessment
    • B. John, and A. Sali Comparative protein structure modeling by iterative alignment, model building and model assessment Nucleic Acids Res. 31 2003 3982 3992
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3982-3992
    • John, B.1    Sali, A.2
  • 46
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • A. Sali, and T.L. Blundell Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2


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