메뉴 건너뛰기




Volumn 10, Issue 1, 2012, Pages 105-116

Key factors in chaperonin-assisted protein folding

Author keywords

Chaperonin; Explicit solvent; Molecular dynamics simulation; Protein folding

Indexed keywords

CHAPERONIN; CHARGE EFFECT; EXPLICIT SOLVENTS; GEOMETRICAL CONFINEMENT EFFECTS; INNER SURFACES; KEY FACTORS; LIVING CELL; MACROMOLECULAR CROWDING; MOLECULAR CHAPERONES; MOLECULAR DYNAMICS SIMULATION; NATIVE STRUCTURES;

EID: 84862789649     PISSN: 16742001     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.partic.2011.02.011     Document Type: Article
Times cited : (9)

References (49)
  • 1
    • 0027316898 scopus 로고
    • To fold or not to fold
    • D.A. Agard To fold or not to fold Science 260 5116 1993 1903 1904
    • (1993) Science , vol.260 , Issue.5116 , pp. 1903-1904
    • Agard, D.A.1
  • 2
    • 0043238073 scopus 로고    scopus 로고
    • Effects of confinement in chaperonin assisted protein folding: Rate enhancement by decreasing the roughness of the folding energy landscape
    • DOI 10.1016/S0022-2836(03)00929-X
    • A. Baumketner, A. Jewett, and J.E. Shea Effects of confinement in chaperonin assisted protein folding: Rate enhancement by decreasing the roughness of the folding energy landscape Journal of Molecular Biology 332 3 2003 701 713 (Pubitemid 37075991)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.3 , pp. 701-713
    • Baumketner, A.1    Jewett, A.2    Shea, J.E.3
  • 6
    • 0035913902 scopus 로고    scopus 로고
    • Dual function of protein confinement in chaperonin-assisted protein folding
    • DOI 10.1016/S0092-8674(01)00517-7
    • A. Brinker, G. Pfeifer, M.J. Kerner, D.J. Naylor, F.U. Hartl, and M. Hayer-Hartl Dual function of protein confinement in chaperonin-assisted protein folding Cell 107 2001 223 233 (Pubitemid 33035948)
    • (2001) Cell , vol.107 , Issue.2 , pp. 223-233
    • Brinker, A.1    Pfeifer, G.2    Kerner, M.J.3    Naylor, D.J.4    Hartl F.Ulrich5    Hayer-Hartl, M.6
  • 7
    • 0034681907 scopus 로고    scopus 로고
    • Unfolding and disassembly of the chaperonin GroEL occurs via a tetradecameric intermediate with a folded equatorial domain
    • DOI 10.1021/bi992619n
    • J. Chen, and D.L. Smith Unfolding and disassembly of the chaperonin GroEL occurs via a tetradecameric intermediate with a folded equatorial domain Biochemistry 39 2000 4250 4258 (Pubitemid 30212640)
    • (2000) Biochemistry , vol.39 , Issue.15 , pp. 4250-4258
    • Chen, J.1    Smith, D.L.2
  • 9
    • 0030816577 scopus 로고    scopus 로고
    • Identification of the predominant non-native histidine ligand in unfolded cytochrome c
    • DOI 10.1021/bi971697c
    • W. Colon, L.P. Wakem, F. Sherman, and H. Roder Identification of the predominant non-native histidine ligand in unfolded cytochrome c Biochemistry 36 1997 12535 12541 (Pubitemid 27446677)
    • (1997) Biochemistry , vol.36 , Issue.41 , pp. 12535-12541
    • Colon, W.1    Wakem, L.P.2    Sherman, F.3    Roder, H.4
  • 10
    • 0034033187 scopus 로고    scopus 로고
    • Long timescale simulations
    • DOI 10.1016/S0959-440X(00)00062-2
    • V. Daggett Long timescale simulations Current Opinion in Structural Biology 10 2000 160 164 (Pubitemid 30198941)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.2 , pp. 160-164
    • Daggett, V.1
  • 11
    • 0035846548 scopus 로고    scopus 로고
    • Molecular chaperones: Inside and outside the Anfinsen cage
    • R.J. Ellis Molecular chaperones: Inside and outside the Anfinsen cage Current Biology 11 2001 1038 1040
    • (2001) Current Biology , vol.11 , pp. 1038-1040
    • Ellis, R.J.1
  • 13
    • 0036632266 scopus 로고    scopus 로고
    • The evolution of the heat-shock protein GroEL from Buchnera, the primary endosymbiont of aphids, is governed by positive selection
    • M.A. Fares, E. Barrio, B. Sabater-Munoz, and A. Moya The evolution of the heat-shock protein GroEL from buchnera, the primary endosymbiont of aphids, is governed by positive selection Molecular Biology and Evolution 19 2002 1162 1170 (Pubitemid 34743240)
    • (2002) Molecular Biology and Evolution , vol.19 , Issue.7 , pp. 1162-1170
    • Fares, M.A.1    Barrio, E.2    Sabater-Munoz, B.3    Moya, A.4
  • 14
    • 0030730821 scopus 로고    scopus 로고
    • Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms
    • G.W. Farr, E.C. Scharl, R.J. Schumacher, S. Sondek, and A.L. Horwich Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms Cell 89 1997 927 937 (Pubitemid 27513519)
    • (1997) Cell , vol.89 , Issue.6 , pp. 927-937
    • Farr, G.W.1    Scharl, E.C.2    Schumacher, R.J.3    Sondek, S.4    Horwich, A.L.5
  • 15
  • 16
    • 0344738987 scopus 로고    scopus 로고
    • Chaperonin-mediated protein folding: Fate of substrate polypeptide
    • DOI 10.1017/S0033583503003883
    • W.A. Fenton, and A.L. Horwich Chaperonin-mediated protein folding: Fate of substrate polypeptide Quarterly Reviews of Biophysics 36 2003 229 256 (Pubitemid 37493574)
    • (2003) Quarterly Reviews of Biophysics , vol.36 , Issue.2 , pp. 229-256
    • Fenton, W.A.1    Horwich, A.L.2
  • 17
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • DOI 10.1038/371614a0
    • W.A. Fenton, Y. Kashi, K. Furtak, and A.L. Norwich Residues in chaperonin GroEL required for polypeptide binding and release Nature 371 1994 614 619 (Pubitemid 24315744)
    • (1994) Nature , vol.371 , Issue.6498 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 18
    • 33748448490 scopus 로고    scopus 로고
    • A natural coarse graining for simulating large biomolecular motion
    • DOI 10.1529/biophysj.106.083568
    • H. Gohlke, and M.F. Thorpe A natural coarse graining for simulating large biomolecular motion Biophysical Journal 91 2006 2115 2120 (Pubitemid 44352394)
    • (2006) Biophysical Journal , vol.91 , Issue.6 , pp. 2115-2120
    • Gohlke, H.1    Thorpe, M.F.2
  • 19
    • 0037040541 scopus 로고    scopus 로고
    • Protein folding. Molecular chaperones in the cytosol: From nascent chain to folded protein
    • DOI 10.1126/science.1068408
    • F.U. Hartl, and M. Hayer-Hartl Molecular chaperones in the cytosol: From nascent chain to folded protein Science 295 2002 1852 1858 (Pubitemid 34214115)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 21
    • 0029186109 scopus 로고
    • Chaperonin-assisted protein folding of the enzyme rhodanese by GroEL/GroES
    • Humana Press New Jersey
    • P.M. Horowitz Chaperonin-assisted protein folding of the enzyme rhodanese by GroEL/GroES Protein stability and folding: Theory and practice 1995 Humana Press New Jersey pp. 361-368
    • (1995) Protein Stability and Folding: Theory and Practice , pp. 361-368
    • Horowitz, P.M.1
  • 23
  • 24
    • 33750000616 scopus 로고    scopus 로고
    • Folding on the Chaperone: Yield Enhancement Through Loose Binding
    • DOI 10.1016/j.jmb.2006.08.040, PII S0022283606010680
    • A.I. Jewett, and J.E. Shea Folding on the chaperone: Yield enhancement through loose binding Journal of Molecular Biology 363 2006 945 957 (Pubitemid 44573225)
    • (2006) Journal of Molecular Biology , vol.363 , Issue.5 , pp. 945-957
    • Jewett, A.I.1    Shea, J.-E.2
  • 25
    • 4444330162 scopus 로고    scopus 로고
    • Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: Creation of an alternate fast folding pathway
    • DOI 10.1073/pnas.0400720101
    • A.I. Jewett, A. Baumketner, and J.E. Shea Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: Creation of an alternate fast folding pathway Proceedings of the National Academy of Sciences of the United States of America 101 2004 13192 13197 (Pubitemid 39209641)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.36 , pp. 13192-13197
    • Jewett, A.I.1    Baumketner, A.2    Shea, J.-E.3
  • 26
    • 0036708447 scopus 로고    scopus 로고
    • Bridging implicit and explicit solvent approaches for membrane electrostatics
    • J.H. Lin, N.A. Baker, and J.A. McCammon Bridging implicit and explicit solvent approaches for membrane electrostatics Biophysical Journal 83 3 2002 1374 1379 (Pubitemid 34977711)
    • (2002) Biophysical Journal , vol.83 , Issue.3 , pp. 1374-1379
    • Lin, J.-H.1    Baker, N.A.2    Andrew McCammon, J.3
  • 27
    • 0030031059 scopus 로고    scopus 로고
    • Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
    • S.C. Mande, V. Mehra, B.R. Bloom, and W.G.J. Hol Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae Science 271 1996 203 207 (5246) (Pubitemid 26033300)
    • (1996) Science , vol.271 , Issue.5246 , pp. 203-207
    • Mande, S.C.1    Mehra, V.2    Bloom, B.R.3    Hol, W.G.J.4
  • 30
    • 0026095524 scopus 로고
    • Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry
    • J.A. Mendoza, G.H. Lorimer, and P.M. Horowitz Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry Journal of Biological Chemistry 266 1991 16973 16976 (Pubitemid 21907891)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.26 , pp. 16973-16976
    • Mendoza, J.A.1    Lorimer, G.H.2    Horowitz, P.M.3
  • 31
    • 0018177366 scopus 로고
    • Structure of bovine liver rhodanese. I. Structure determination at 2.5 A resolution and a comparison of the conformation and sequence of its two domains
    • DOI 10.1016/0022-2836(78)90207-3
    • J.H. Ploegman, G. Drent, K.H. Kalk, and W.G. Hol Structure of bovine liver rhodanese. I. Structure determination at 2.5 A resolution and a comparison of the conformation and sequence of its two domains Journal of Molecular Biology 123 1978 557 594 (Pubitemid 9006587)
    • (1978) Journal of Molecular Biology , vol.123 , Issue.4 , pp. 557-594
    • Ploegman, J.H.1    Drent, G.2    Kalk, K.H.3    Hol, W.G.J.4
  • 32
    • 33646144221 scopus 로고    scopus 로고
    • Confinement effects on the thermodynamics of protein folding: Monte Carlo simulations
    • N. Rathore, T.A. Knotts, and J.J. de Pablo Confinement effects on the thermodynamics of protein folding: Monte Carlo simulations Biophysical Journal 90 2006 1767 1773
    • (2006) Biophysical Journal , vol.90 , pp. 1767-1773
    • Rathore, N.1    Knotts, T.A.2    De Pablo, J.J.3
  • 33
    • 67349084347 scopus 로고    scopus 로고
    • Explicit solvent molecular dynamics simulations of chaperonin-assisted rhodanese folding
    • Y. Ren, J. Gao, J. Xu, W. Ge, and J. Li Explicit solvent molecular dynamics simulations of chaperonin-assisted rhodanese folding Particuology 7 3 2009 220 224
    • (2009) Particuology , vol.7 , Issue.3 , pp. 220-224
    • Ren, Y.1    Gao, J.2    Xu, J.3    Ge, W.4    Li, J.5
  • 34
    • 70349680408 scopus 로고    scopus 로고
    • Thermal unfolding of a double-domain protein: Molecular dynamics simulation of rhodanese
    • Y. Ren, J. Gao, W. Ge, and J. Li Thermal unfolding of a double-domain protein: Molecular dynamics simulation of rhodanese Industrial & Engineering Chemistry Research 48 19 2009 8865 8871
    • (2009) Industrial & Engineering Chemistry Research , vol.48 , Issue.19 , pp. 8865-8871
    • Ren, Y.1    Gao, J.2    Ge, W.3    Li, J.4
  • 35
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
    • DOI 10.1016/S0092-8674(00)80742-4
    • H.S. Rye, A.M. Roseman, S. Chen, K. Furtak, W.A. Fenton, and H.R. Saibil GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings Cell 97 1999 325 338 (Pubitemid 29214589)
    • (1999) Cell , vol.97 , Issue.3 , pp. 325-338
    • Rye, H.S.1    Roseman, A.M.2    Chen, S.3    Furtak, K.4    Fenton, W.A.5    Saibil, H.R.6    Horwich, A.L.7
  • 36
    • 0033617534 scopus 로고    scopus 로고
    • Chaperonin function: Folding by forced unfolding
    • DOI 10.1126/science.284.5415.822
    • M. Shtilerman, G.H. Lorimer, and E.S. Walter Chaperonin function: Folding by forced unfolding Science 284 1999 822 825 (Pubitemid 29291351)
    • (1999) Science , vol.284 , Issue.5415 , pp. 822-825
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 38
    • 20544466881 scopus 로고    scopus 로고
    • Probing the "annealing" mechanism of GroEL minichaperone using molecular dynamics simulations
    • DOI 10.1016/j.jmb.2005.05.012, PII S0022283605005322
    • G. Stan, B.R. Brooks, and D. Thirumalai Probing the "annealing" mechanism of GroEL minichaperone using molecular dynamics simulations Journal of Molecular Biology 350 2005 817 829 (Pubitemid 40848677)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.4 , pp. 817-829
    • Stan, G.1    Brooks, B.R.2    Thirumalai, D.3
  • 39
    • 0035783334 scopus 로고    scopus 로고
    • Review: Nucleotide binding to the thermoplasma thermosome: Implications for the functional cycle of group II chaperonins
    • S. Steinbacher, and L. Ditzel Review: Nucleotide binding to the thermoplasma thermosome: Implications for the functional cycle of group II chaperonins Journal of Structural Biology 135 2001 147 156
    • (2001) Journal of Structural Biology , vol.135 , pp. 147-156
    • Steinbacher, S.1    Ditzel, L.2
  • 40
    • 0141482088 scopus 로고    scopus 로고
    • How protein thermodynamics and folding mechanisms are altered by the chaperonin cage: Molecular simulations
    • DOI 10.1073/pnas.1831920100
    • F. Takagi, N. Koga, and S. Takada How protein thermodynamics and folding mechanisms are altered by the chaperonin cage: Molecular simulations Proceedings of the National Academy of Sciences of the United States of America 100 2003 11367 11372 (Pubitemid 37205941)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.20 , pp. 11367-11372
    • Takagi, F.1    Koga, N.2    Takada, S.3
  • 41
    • 33646897305 scopus 로고    scopus 로고
    • Structural Features of the GroEL-GroES Nano-Cage Required for Rapid Folding of Encapsulated Protein
    • DOI 10.1016/j.cell.2006.04.027, PII S0092867406005605
    • Y.C. Tang, H.C. Chang, A. Roeben, D. Wischnewski, N. Wischnewski, and M.J. Kerner Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein Cell 125 2006 903 914 (Pubitemid 43795198)
    • (2006) Cell , vol.125 , Issue.5 , pp. 903-914
    • Tang, Y.-C.1    Chang, H.-C.2    Roeben, A.3    Wischnewski, D.4    Wischnewski, N.5    Kerner, M.J.6    Hartl, F.U.7    Hayer-Hartl, M.8
  • 42
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
    • M.J. Todd, P.V. Viitanen, and G.H. Lorimer Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding Science 265 1994 659 666 (Pubitemid 24268276)
    • (1994) Science , vol.265 , Issue.5172 , pp. 659-666
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 44
    • 3042856284 scopus 로고    scopus 로고
    • The unfolding action of GroEL on a protein substrate
    • DOI 10.1529/biophysj.103.037333
    • A. van der Vaart, J. Ma, and M. Karplus The unfolding action of GroEL on a protein substrate Biophysical Journal 87 2004 562 573 (Pubitemid 38880109)
    • (2004) Biophysical Journal , vol.87 , Issue.1 , pp. 562-573
    • Van Der Vaart, A.1    Ma, J.2    Karplus, M.3
  • 45
    • 0037184939 scopus 로고    scopus 로고
    • Directed evolution of substrate-optimized GroEL/S chaperonins
    • DOI 10.1016/S0092-8674(02)01198-4
    • J.D. Wang, C. Herman, K.A. Tipton, C.A. Gross, and J.S. Weissman Directed evolution of substrate-optimized GroEL/S chaperonins Cell 111 2002 1027 1039 (Pubitemid 36044693)
    • (2002) Cell , vol.111 , Issue.7 , pp. 1027-1039
    • Wang, J.D.1    Herman, C.2    Tipton, K.A.3    Gross, C.A.4    Weissman, J.S.5
  • 46
    • 28644434901 scopus 로고    scopus 로고
    • Folding behavior of chaperonin-mediated substrate protein
    • DOI 10.1002/prot.20689
    • W.X. Xu, J. Wang, and W. Wang Folding behavior of chaperonin-mediated substrate protein Proteins: Structure, Function, and Bioinformatics 61 4 2005 777 794 (Pubitemid 41753149)
    • (2005) Proteins: Structure, Function and Genetics , vol.61 , Issue.4 , pp. 777-794
    • Xu, W.-X.1    Wang, J.2    Wang, W.3
  • 47
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 48
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • DOI 10.1038/41944
    • Z. Xu, A.L. Horwich, and P.B. Sigler The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex Nature 388 1997 741 750 (Pubitemid 27375147)
    • (1997) Nature , vol.388 , Issue.6644 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.