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Volumn 112, Issue 31, 2015, Pages E4206-E4215

Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone

Author keywords

DnaK; Hsp70; Molecular chaperone; Protein folding; Triple resonance NMR

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70; PROTEIN DNAK; PROTEIN SH3; ADENOSINE DIPHOSPHATE; DNAK PROTEIN, E COLI; DRK PROTEIN, DROSOPHILA; DROSOPHILA PROTEIN; ESCHERICHIA COLI PROTEIN; PROTEIN BINDING; SOLVENT;

EID: 84938717684     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1505173112     Document Type: Article
Times cited : (50)

References (46)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181(4096):223-230.
    • (1973) Science , vol.181 , Issue.4096 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 84886412961 scopus 로고    scopus 로고
    • Chaperone machines for protein folding, unfolding and disaggregation
    • Saibil H (2013) Chaperone machines for protein folding, unfolding and disaggregation. Nat Rev Mol Cell Biol 14(10):630-642.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , Issue.10 , pp. 630-642
    • Saibil, H.1
  • 4
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B, Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92(3):351-366.
    • (1998) Cell , vol.92 , Issue.3 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 6
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ, Sambrook J (1992) Protein folding in the cell. Nature 355(6355):33-45.
    • (1992) Nature , vol.355 , Issue.6355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 8
    • 84874473589 scopus 로고    scopus 로고
    • Allostery in the Hsp70 chaperone proteins
    • Zuiderweg ER, et al. (2013) Allostery in the Hsp70 chaperone proteins. Top Curr Chem 328:99-153.
    • (2013) Top Curr Chem , vol.328 , pp. 99-153
    • Zuiderweg, E.R.1
  • 9
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: Localized functions of cytosolic chaperones
    • Young JC, Barral JM, Ulrich Hartl F (2003) More than folding: Localized functions of cytosolic chaperones. Trends Biochem Sci 28(10):541-547.
    • (2003) Trends Biochem Sci , vol.28 , Issue.10 , pp. 541-547
    • Young, J.C.1    Barral, J.M.2    Ulrich Hartl, F.3
  • 10
    • 84878964181 scopus 로고    scopus 로고
    • The HSP70 family and cancer
    • Murphy ME (2013) The HSP70 family and cancer. Carcinogenesis 34(6):1181-1188.
    • (2013) Carcinogenesis , vol.34 , Issue.6 , pp. 1181-1188
    • Murphy, M.E.1
  • 11
    • 0030054050 scopus 로고    scopus 로고
    • T cell lymphoma in transgenic mice expressing the human Hsp70 gene
    • Seo JS, et al. (1996) T cell lymphoma in transgenic mice expressing the human Hsp70 gene. Biochem Biophys Res Commun 218(2):582-587.
    • (1996) Biochem Biophys Res Commun , vol.218 , Issue.2 , pp. 582-587
    • Seo, J.S.1
  • 12
    • 33845918172 scopus 로고    scopus 로고
    • Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro
    • Evans CG, Wisén S, Gestwicki JE (2006) Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro. J Biol Chem 281(44):33182-33191.
    • (2006) J Biol Chem , vol.281 , Issue.44 , pp. 33182-33191
    • Evans, C.G.1    Wisén, S.2    Gestwicki, J.E.3
  • 13
    • 0037014426 scopus 로고    scopus 로고
    • Protein misfolding, amyloid formation, and neurodegeneration: A critical role for molecular chaperones?
    • Muchowski PJ (2002) Protein misfolding, amyloid formation, and neurodegeneration: A critical role for molecular chaperones? Neuron 35(1):9-12.
    • (2002) Neuron , vol.35 , Issue.1 , pp. 9-12
    • Muchowski, P.J.1
  • 14
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski PJ, Wacker JL (2005) Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 6(1):11-22.
    • (2005) Nat Rev Neurosci , vol.6 , Issue.1 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 15
    • 84870916379 scopus 로고    scopus 로고
    • An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones
    • Zhuravleva A, Clerico EM, Gierasch LM (2012) An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell 151(6): 1296-1307.
    • (2012) Cell , vol.151 , Issue.6 , pp. 1296-1307
    • Zhuravleva, A.1    Clerico, E.M.2    Gierasch, L.M.3
  • 16
    • 84924139172 scopus 로고    scopus 로고
    • How Hsp70 molecular machines interact with their substrates to mediate diverse physiological functions
    • Clerico EM, Tilitsky JM, Meng W, Gierasch LM (2015) How Hsp70 molecular machines interact with their substrates to mediate diverse physiological functions. J Mol Biol 42(7):1575-1588.
    • (2015) J Mol Biol , vol.42 , Issue.7 , pp. 1575-1588
    • Clerico, E.M.1    Tilitsky, J.M.2    Meng, W.3    Gierasch, L.M.4
  • 17
    • 84884589727 scopus 로고    scopus 로고
    • Hsp70 chaperone dynamics and molecular mechanism
    • Mayer MP (2013) Hsp70 chaperone dynamics and molecular mechanism. Trend Biochem Sci 38(10):507-514.
    • (2013) Trend Biochem Sci , vol.38 , Issue.10 , pp. 507-514
    • Mayer, M.P.1
  • 18
    • 0029937037 scopus 로고    scopus 로고
    • Structural analysis of substrate binding by the molecular chaperone DnaK
    • Zhu X, et al. (1996) Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272(5268):1606-1614.
    • (1996) Science , vol.272 , Issue.5268 , pp. 1606-1614
    • Zhu, X.1
  • 19
    • 0026595140 scopus 로고
    • Different conformations for the same polypeptide bound to chaperones DnaK and GroEL
    • Landry SJ, Jordan R, McMacken R, Gierasch LM (1992) Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature 355(6359):455-457.
    • (1992) Nature , vol.355 , Issue.6359 , pp. 455-457
    • Landry, S.J.1    Jordan, R.2    McMacken, R.3    Gierasch, L.M.4
  • 20
    • 15244340796 scopus 로고    scopus 로고
    • Structural dynamics of the DnaK-peptide complex
    • Popp S, et al. (2005) Structural dynamics of the DnaK-peptide complex. J Mol Biol 347(5):1039-1052.
    • (2005) J Mol Biol , vol.347 , Issue.5 , pp. 1039-1052
    • Popp, S.1
  • 21
    • 33749512433 scopus 로고    scopus 로고
    • Secondary structure mapping of DnaK-bound protein fragments: Chain helicity and local helix unwinding at the binding site
    • Chen Z, Kurt N, Rajagopalan S, Cavagnero S (2006) Secondary structure mapping of DnaK-bound protein fragments: Chain helicity and local helix unwinding at the binding site. Biochemistry 45(40):12325-12333.
    • (2006) Biochemistry , vol.45 , Issue.40 , pp. 12325-12333
    • Chen, Z.1    Kurt, N.2    Rajagopalan, S.3    Cavagnero, S.4
  • 22
    • 41649088672 scopus 로고    scopus 로고
    • Nonnative helical motif in a chaperone-bound protein fragment
    • Kurt N, Cavagnero S (2008) Nonnative helical motif in a chaperone-bound protein fragment. Biophys J 94(7):L48-L50.
    • (2008) Biophys J , vol.94 , Issue.7 , pp. L48-L50
    • Kurt, N.1    Cavagnero, S.2
  • 23
    • 84866139470 scopus 로고    scopus 로고
    • Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU)
    • Kim JH, Tonelli M, Frederick RO, Chow DC-F, Markley JL (2012) Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU). J Biol Chem 287(37):31406-31413.
    • (2012) J Biol Chem , vol.287 , Issue.37 , pp. 31406-31413
    • Kim, J.H.1    Tonelli, M.2    Frederick, R.O.3    Chow, D.C.-F.4    Markley, J.L.5
  • 24
    • 0026700861 scopus 로고
    • Protein folding and protein refolding
    • Seckler R, Jaenicke R (1992) Protein folding and protein refolding. FASEB J 6(8): 2545-2552.
    • (1992) FASEB J , vol.6 , Issue.8 , pp. 2545-2552
    • Seckler, R.1    Jaenicke, R.2
  • 25
    • 84862580407 scopus 로고    scopus 로고
    • Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery
    • Sekhar A, Santiago M, Lam HN, Lee JH, Cavagnero S (2012) Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery. Protein Sci 21(7): 1042-1055.
    • (2012) Protein Sci , vol.21 , Issue.7 , pp. 1042-1055
    • Sekhar, A.1    Santiago, M.2    Lam, H.N.3    Lee, J.H.4    Cavagnero, S.5
  • 26
    • 84878901297 scopus 로고    scopus 로고
    • Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides
    • Priya S, Sharma SK, Goloubinoff P (2013) Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides. FEBS Lett 587(13):1981-1987.
    • (2013) FEBS Lett , vol.587 , Issue.13 , pp. 1981-1987
    • Priya, S.1    Sharma, S.K.2    Goloubinoff, P.3
  • 27
    • 0036049850 scopus 로고    scopus 로고
    • The unfolding story of the Escherichia coli Hsp70 DnaK: Is DnaK a holdase or an unfoldase?
    • Slepenkov SV, Witt SN (2002) The unfolding story of the Escherichia coli Hsp70 DnaK: Is DnaK a holdase or an unfoldase? Mol Microbiol 45(5):1197-1206.
    • (2002) Mol Microbiol , vol.45 , Issue.5 , pp. 1197-1206
    • Slepenkov, S.V.1    Witt, S.N.2
  • 28
    • 0028541866 scopus 로고
    • Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • Zhang O, Kay LE, Olivier JP, Forman-Kay JD (1994) Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR 4(6): 845-858.
    • (1994) J Biomol NMR , vol.4 , Issue.6 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 29
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rüdiger S, Germeroth L, Schneider-Mergener J, Bukau B (1997) Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J 16(7):1501-1507.
    • (1997) EMBO J , vol.16 , Issue.7 , pp. 1501-1507
    • Rüdiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 30
    • 33751212795 scopus 로고    scopus 로고
    • Binding specificity of an alpha-helical protein sequence to a full-length Hsp70 chaperone and its minimal substrate-binding domain
    • Vega CA, Kurt N, Chen Z, Rüdiger S, Cavagnero S (2006) Binding specificity of an alpha-helical protein sequence to a full-length Hsp70 chaperone and its minimal substrate-binding domain. Biochemistry 45(46):13835-13846.
    • (2006) Biochemistry , vol.45 , Issue.46 , pp. 13835-13846
    • Vega, C.A.1    Kurt, N.2    Chen, Z.3    Rüdiger, S.4    Cavagnero, S.5
  • 31
    • 70049103049 scopus 로고    scopus 로고
    • Accurate prediction of DnaK-peptide binding via homology modelling and experimental data
    • Van Durme J, et al. (2009) Accurate prediction of DnaK-peptide binding via homology modelling and experimental data. PLoS Comput Biol 5(8):e1000475.
    • (2009) PLoS Comput Biol , vol.5 , Issue.8
    • Van Durme, J.1
  • 32
    • 0033996510 scopus 로고    scopus 로고
    • Identification of a Hsp70 recognition domain within the rubisco small subunit transit peptide
    • Ivey RA, 3rd, Subramanian C, Bruce BD (2000) Identification of a Hsp70 recognition domain within the rubisco small subunit transit peptide. Plant Physiol 122(4): 1289-1299.
    • (2000) Plant Physiol , vol.122 , Issue.4 , pp. 1289-1299
    • Ivey, R.A.1    Subramanian, C.2    Bruce, B.D.3
  • 33
    • 84866621300 scopus 로고    scopus 로고
    • Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system
    • Sekhar A, Lam HN, Cavagnero S (2012) Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system. Protein Sci 21(10):1489-1502.
    • (2012) Protein Sci , vol.21 , Issue.10 , pp. 1489-1502
    • Sekhar, A.1    Lam, H.N.2    Cavagnero, S.3
  • 34
    • 0000752185 scopus 로고
    • Effects of chemical-exchange in diffusion-ordered 2D NMR-spectra
    • Johnson CS (1993) Effects of chemical-exchange in diffusion-ordered 2D NMR-spectra. J Magn Reson A 102(2):214-218.
    • (1993) J Magn Reson a , vol.102 , Issue.2 , pp. 214-218
    • Johnson, C.S.1
  • 35
    • 34047268015 scopus 로고    scopus 로고
    • Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker
    • Swain JF, et al. (2007) Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Mol Cell 26(1):27-39.
    • (2007) Mol Cell , vol.26 , Issue.1 , pp. 27-39
    • Swain, J.F.1
  • 36
    • 0036700882 scopus 로고    scopus 로고
    • Clean SEA-HSQC: A method to map solvent exposed amides in large non-deuterated proteins with gradient-enhanced HSQC
    • Lin D, Sze KH, Cui Y, Zhu G (2002) Clean SEA-HSQC: A method to map solvent exposed amides in large non-deuterated proteins with gradient-enhanced HSQC. J Biomol NMR 23(4):317-322.
    • (2002) J Biomol NMR , vol.23 , Issue.4 , pp. 317-322
    • Lin, D.1    Sze, K.H.2    Cui, Y.3    Zhu, G.4
  • 37
    • 0031989849 scopus 로고    scopus 로고
    • Accurate quantitation of water-amide proton exchange rates using the phase-modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme
    • Hwang TL, van Zijl PCM, Mori S (1998) Accurate quantitation of water-amide proton exchange rates using the phase-modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme. J Biomol NMR 11(2):221-226.
    • (1998) J Biomol NMR , vol.11 , Issue.2 , pp. 221-226
    • Hwang, T.L.1    Van Zijl, P.C.M.2    Mori, S.3
  • 38
    • 0030797606 scopus 로고    scopus 로고
    • Application of phase-modulated CLEAN chemical EXchange spectroscopy (CLEANEX-PM) to detect water-protein proton exchange and intermolecular NOEs
    • Hwang TL, Mori S, Shaka AJ, vanZijl PCM (1997) Application of phase-modulated CLEAN chemical EXchange spectroscopy (CLEANEX-PM) to detect water-protein proton exchange and intermolecular NOEs. J Am Chem Soc 119(26):6203-6204.
    • (1997) J Am Chem Soc , vol.119 , Issue.26 , pp. 6203-6204
    • Hwang, T.L.1    Mori, S.2    Shaka, A.J.3    VanZijl, P.C.M.4
  • 39
    • 78649309029 scopus 로고    scopus 로고
    • The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
    • Sharma SK, De los Rios P, Christen P, Lustig A, Goloubinoff P (2010) The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. Nat Chem Biol 6(12):914-920.
    • (2010) Nat Chem Biol , vol.6 , Issue.12 , pp. 914-920
    • Sharma, S.K.1    De Los Rios, P.2    Christen, P.3    Lustig, A.4    Goloubinoff, P.5
  • 40
    • 84907186821 scopus 로고    scopus 로고
    • Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein
    • Kellner R, et al. (2014) Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein. Proc Natl Acad Sci USA 111(37):13355-13360.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.37 , pp. 13355-13360
    • Kellner, R.1
  • 41
    • 84902326560 scopus 로고    scopus 로고
    • Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption
    • De Los Rios P, Barducci A (2014) Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption. eLife 3:e02218.
    • (2014) eLife , vol.3
    • De Los Rios, P.1    Barducci, A.2
  • 42
    • 64649094781 scopus 로고    scopus 로고
    • Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
    • Bertelsen EB, Chang L, Gestwicki JE, Zuiderweg ERP (2009) Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc Natl Acad Sci USA 106(21):8471-8476.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.21 , pp. 8471-8476
    • Bertelsen, E.B.1    Chang, L.2    Gestwicki, J.E.3    Zuiderweg, E.R.P.4
  • 43
  • 44
    • 28244434114 scopus 로고    scopus 로고
    • Structural comparison of the unstable drkN SH3 domain and a stable mutant
    • Bezsonova I, Singer A, Choy WY, Tollinger M, Forman-Kay JD (2005) Structural comparison of the unstable drkN SH3 domain and a stable mutant. Biochemistry 44(47): 15550-15560.
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15550-15560
    • Bezsonova, I.1    Singer, A.2    Choy, W.Y.3    Tollinger, M.4    Forman-Kay, J.D.5
  • 45
    • 0001424822 scopus 로고    scopus 로고
    • Suppression of convection artifacts in stimulated-echo diffusion experiments. Double-stimulated-echo experiments
    • Jerschow A, Muller N (1997) Suppression of convection artifacts in stimulated-echo diffusion experiments. Double-stimulated-echo experiments. J Magn Reson 125(2): 372-375.
    • (1997) J Magn Reson , vol.125 , Issue.2 , pp. 372-375
    • Jerschow, A.1    Muller, N.2
  • 46
    • 0036437145 scopus 로고    scopus 로고
    • A one-shot sequence for high-resolution diffusion-ordered spectroscopy
    • Pelta MD, Morris GA, Stchedroff MJ, Hammond SJ (2002) A one-shot sequence for high-resolution diffusion-ordered spectroscopy. Magn Reson Chem 40(13):S147-S152.
    • (2002) Magn Reson Chem , vol.40 , Issue.13 , pp. S147-S152
    • Pelta, M.D.1    Morris, G.A.2    Stchedroff, M.J.3    Hammond, S.J.4


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