메뉴 건너뛰기




Volumn 100, Issue 1-3, 2002, Pages 453-467

Annealing function of GroEL: Structural and bioinformatic analysis

Author keywords

Annealing; Chaperonin function; Escherichia coli; GroEL

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CHAPERONIN; HEAT SHOCK PROTEIN 60; NUCLEOTIDE; PEPTIDE; PROTEIN;

EID: 0037438479     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00298-3     Document Type: Article
Times cited : (37)

References (38)
  • 1
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • Fenton W.A., Horwich A.L. GroEL-mediated protein folding. Prot. Sci. 6:2000;743-760.
    • (2000) Prot. Sci. , vol.6 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 2
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K.A., Chan H.S. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4:1997;10-19.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 4
    • 0001103473 scopus 로고    scopus 로고
    • Kinetics of folding of proteins and RNA
    • Thirumalai D., Woodson S.A. Kinetics of folding of proteins and RNA. Acc. Chem. Res. 29:1996;433-439.
    • (1996) Acc. Chem. Res. , vol.29 , pp. 433-439
    • Thirumalai, D.1    Woodson, S.A.2
  • 5
    • 0034652350 scopus 로고    scopus 로고
    • Coupling between protein folding and allostery in the GroE chaperonin system
    • Yifrach O., Horovitz A. Coupling between protein folding and allostery in the GroE chaperonin system. Proc. Natl. Acad. Sci. USA. 97:2000;1521-1524.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1521-1524
    • Yifrach, O.1    Horovitz, A.2
  • 6
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implication for facilitated protein folding
    • Todd M.J., Viitanen P.V., Lorimer G.H. Dynamics of the chaperonin ATPase cycle: implication for facilitated protein folding. Science. 256:1994;659-666.
    • (1994) Science , vol.256 , pp. 659-666
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 7
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
    • Rye H.S., Roseman A.M., Chen S., Funak K., Fenton W.A., Saibil H.R., Horwich A.L. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell. 97:1999;325-338.
    • (1999) Cell , vol.97 , pp. 325-338
    • Rye, H.S.1    Roseman, A.M.2    Chen, S.3    Funak, K.4    Fenton, W.A.5    Saibil, H.R.6    Horwich, A.L.7
  • 9
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
    • Hunt J.F., Weaver A.J., Landry S.J., Gierasch L., Diesenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature. 379:1996;37-45.
    • (1996) Nature , vol.379 , pp. 37-45
    • Hunt, J.F.1    Weaver, A.J.2    Landry, S.J.3    Gierasch, L.4    Diesenhofer, J.5
  • 14
    • 0033515436 scopus 로고    scopus 로고
    • Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity
    • Betancourt M.R., Thirumalai D. Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity. J. Mol. Biol. 287:1999;627-644.
    • (1999) J. Mol. Biol. , vol.287 , pp. 627-644
    • Betancourt, M.R.1    Thirumalai, D.2
  • 15
    • 0030006212 scopus 로고    scopus 로고
    • Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism
    • Todd M.J., Lorimer G.H., Thirumalai D. Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc. Natl. Acad. Sci. USA. 93:1996;4030-4035.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4030-4035
    • Todd, M.J.1    Lorimer, G.H.2    Thirumalai, D.3
  • 16
  • 17
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton W.A., Kashi Y., Furtak K., Horwich A.L. Residues in chaperonin GroEL required for polypeptide binding and release. Nature. 371:1994;614-619.
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 18
    • 0033598941 scopus 로고    scopus 로고
    • The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
    • Chen L.L., Sigler P.B. The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity. Cell. 99:1999;757-768.
    • (1999) Cell , vol.99 , pp. 757-768
    • Chen, L.L.1    Sigler, P.B.2
  • 19
  • 20
    • 0030061845 scopus 로고    scopus 로고
    • Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
    • Zahn R., Perrett S., Stenberg G., Fersht A.R. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Science. 271:1996;642-645.
    • (1996) Science , vol.271 , pp. 642-645
    • Zahn, R.1    Perrett, S.2    Stenberg, G.3    Fersht, A.R.4
  • 21
    • 0033617534 scopus 로고    scopus 로고
    • Chaperonin function: Folding by forced unfolding
    • Shtilerman M., Lorimer G.H., Englander S.W. Chaperonin function: folding by forced unfolding. Science. 284:1999;822-825.
    • (1999) Science , vol.284 , pp. 822-825
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 22
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B., Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55:1971;379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 24
    • 0028362702 scopus 로고
    • Prediction of an inter-residue in the chaperonin GroEL from multiple sequence alignment is confirmed by double-mutant cycle analysis
    • Horovitz A., Bochkareva E.S., Yifrach O., Girshovich A.S. Prediction of an inter-residue in the chaperonin GroEL from multiple sequence alignment is confirmed by double-mutant cycle analysis. J. Mol. Biol. 238:1994;133-138.
    • (1994) J. Mol. Biol. , vol.238 , pp. 133-138
    • Horovitz, A.1    Bochkareva, E.S.2    Yifrach, O.3    Girshovich, A.S.4
  • 25
    • 0012459508 scopus 로고    scopus 로고
    • Structural models of GroEL do not include 23 carboxy-terminal residues, which are not visible in the available crystal structures [8, 11, 30]
    • Structural models of GroEL do not include 23 carboxy-terminal residues, which are not visible in the available crystal structures [8, 11, 30].
  • 26
    • 0028785583 scopus 로고
    • Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
    • Weissman J.S., Rye H.S., Fenton W.A., Beechem J.M., Horwich A.L. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell. 83:1995;577-587.
    • (1995) Cell , vol.83 , pp. 577-587
    • Weissman, J.S.1    Rye, H.S.2    Fenton, W.A.3    Beechem, J.M.4    Horwich, A.L.5
  • 27
    • 0034064511 scopus 로고    scopus 로고
    • Conservation among HSP60 sequences in relation to structure, function, and evolution
    • Brocchieri L., Karlin S. Conservation among HSP60 sequences in relation to structure, function, and evolution. Prot. Sci. 9:2000;476-486.
    • (2000) Prot. Sci. , vol.9 , pp. 476-486
    • Brocchieri, L.1    Karlin, S.2
  • 28
    • 0012370037 scopus 로고    scopus 로고
    • private communication
    • J.F. Hunt, private communication.
    • Hunt, J.F.1
  • 30
    • 0029664944 scopus 로고    scopus 로고
    • The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP-γS
    • Boisvert D.C., Wang J., Otwinowski Z., Horwich A.L., Sigler P.B. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP-γS. Nat. Struct. Biol. 3:1996;170-177.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 170-177
    • Boisvert, D.C.1    Wang, J.2    Otwinowski, Z.3    Horwich, A.L.4    Sigler, P.B.5
  • 31
    • 0036721218 scopus 로고    scopus 로고
    • Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations'
    • Kass I., Horovitz A. Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations'. Prot.: Struct. Funct. Genet. 48:2002;611-617.
    • (2002) Prot.: Struct. Funct. Genet. , vol.48 , pp. 611-617
    • Kass, I.1    Horovitz, A.2
  • 32
    • 0034665864 scopus 로고    scopus 로고
    • A dynamic model for the allosteric mechanism of GroEL
    • Ma J.P., Siegler P.B., Xu Z., Karplus M. A dynamic model for the allosteric mechanism of GroEL. J. Mol. Biol. 302:2000;303-313.
    • (2000) J. Mol. Biol. , vol.302 , pp. 303-313
    • Ma, J.P.1    Siegler, P.B.2    Xu, Z.3    Karplus, M.4
  • 33
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24:1991;946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 34
    • 0012453620 scopus 로고    scopus 로고
    • Povscript was written by Dan Peisach of Brandeis University
    • Povscript was written by Dan Peisach of Brandeis University.
  • 36
    • 0034284122 scopus 로고    scopus 로고
    • Recent changes to RasMol, recombining the variants
    • Bernstein H.J. Recent changes to RasMol, recombining the variants. Trends Biochem. Sci. 25:2000;453-455.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 453-455
    • Bernstein, H.J.1
  • 37
    • 85068245557 scopus 로고    scopus 로고
    • ®
    • ®.
  • 38
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg D., Schwartz E., Komaromy M., Wall R. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179:1984;125-142.
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwartz, E.2    Komaromy, M.3    Wall, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.