메뉴 건너뛰기




Volumn 334, Issue 3, 2003, Pages 489-499

Domain motions in GroEL upon binding of an oligopeptide

Author keywords

Domain motions; Intra ring negative allostery; Opposite allosteric effectors; Symmetric GroEL complex

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; CHAPERONIN; OLIGOPEPTIDE; PEPTIDE; PROTEIN SUBUNIT;

EID: 0242493845     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.074     Document Type: Article
Times cited : (44)

References (45)
  • 3
    • 0027065105 scopus 로고
    • Purified chaperonin 60 (GroEL) interacts with the non-native states of a multitude of Escherichia coli proteins
    • Viitanen P.V., Gatenby A.A., Lorimer G.H. Purified chaperonin 60 (GroEL) interacts with the non-native states of a multitude of Escherichia coli proteins. Protein Sci. 1:1992;363-369.
    • (1992) Protein Sci. , vol.1 , pp. 363-369
    • Viitanen, P.V.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 4
    • 0027214204 scopus 로고
    • Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
    • Horwich A.L., Low K.B., Fenton W.A., Hirshfield I.N., Furtak K. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell. 74:1993;909-917.
    • (1993) Cell , vol.74 , pp. 909-917
    • Horwich, A.L.1    Low, K.B.2    Fenton, W.A.3    Hirshfield, I.N.4    Furtak, K.5
  • 6
    • 85047684938 scopus 로고    scopus 로고
    • Mechanism of substrate recognition by the chaperonin GroEL
    • Houry W.A. Mechanism of substrate recognition by the chaperonin GroEL. Biochem. Cell Biol. 79:2001;569-577.
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 569-577
    • Houry, W.A.1
  • 9
    • 0028113299 scopus 로고
    • Residues in GroEL required for polypeptide binding and release
    • Fenton W.A., Kashi Y., Furtak K., Horwich A.L. Residues in 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
  • 10
    • 0030966765 scopus 로고    scopus 로고
    • A structural model for GroEL-polypeptide recognition
    • Buckle A.M., Zahn R., Fersht A.R. A structural model for GroEL-polypeptide recognition. Proc. Natl Acad. Sci. USA. 94:1997;3571-3575.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3571-3575
    • Buckle, A.M.1    Zahn, R.2    Fersht, A.R.3
  • 11
    • 0033598941 scopus 로고    scopus 로고
    • The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
    • Chen 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.1    Sigler, P.B.2
  • 12
    • 0034685612 scopus 로고    scopus 로고
    • Stabilization of GroEL minichaperones by core and surface mutations
    • Wang Q., Buckle A.M., Fersht A.R. Stabilization of GroEL minichaperones by core and surface mutations. J. Mol. Biol. 298:2000;917-926.
    • (2000) J. Mol. Biol. , vol.298 , pp. 917-926
    • Wang, Q.1    Buckle, A.M.2    Fersht, A.R.3
  • 13
    • 0034671446 scopus 로고    scopus 로고
    • From minichaperone to GroEL 1: Information on GroEL-polypeptide interactions from crystal packing of minichaperones
    • Wang Q., Buckle A.M., Fersht A.R. From minichaperone to GroEL 1: information on GroEL-polypeptide interactions from crystal packing of minichaperones. J. Mol. Biol. 304:2000;873-881.
    • (2000) J. Mol. Biol. , vol.304 , pp. 873-881
    • Wang, Q.1    Buckle, A.M.2    Fersht, A.R.3
  • 15
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z., Horwich A.L., Sigler P.B. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature. 388:1997;741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 16
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES cochaperonin at 2.8 Å resolution
    • Hunt J.F., Weaver A.J., Landry S.J., Gierasch L., Deisenhofer J. The crystal structure of the GroES cochaperonin 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    Deisenhofer, J.5
  • 17
    • 0030024540 scopus 로고    scopus 로고
    • Structure of the heat shock protein chaperonin-10 of Mycobacterium laprae
    • Mande S.C., Mehra V., Bloom B.R., Hol W.G.J. Structure of the heat shock protein chaperonin-10 of Mycobacterium laprae. Science. 271:1996;203-207.
    • (1996) Science , vol.271 , pp. 203-207
    • Mande, S.C.1    Mehra, V.2    Bloom, B.R.3    Hol, W.G.J.4
  • 18
    • 0028027055 scopus 로고
    • Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy
    • Chen S., Roseman A.M., Hunter A.S., Wood S.P., Burton S.G., Ranson N.A., et al. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature. 371:1994;261-264.
    • (1994) Nature , vol.371 , pp. 261-264
    • Chen, S.1    Roseman, A.M.2    Hunter, A.S.3    Wood, S.P.4    Burton, S.G.5    Ranson, N.A.6
  • 20
    • 0028071381 scopus 로고
    • Symmetric complexes of GroE chaperonins as part of the functional cycle
    • Schmidt M., Rutkat K., Rachel R., Pfeifer G., Jaenicke R., Viitanen P., et al. Symmetric complexes of GroE chaperonins as part of the functional cycle. Science. 265:1994;656-659.
    • (1994) Science , vol.265 , pp. 656-659
    • Schmidt, M.1    Rutkat, K.2    Rachel, R.3    Pfeifer, G.4    Jaenicke, R.5    Viitanen, P.6
  • 21
    • 0031037687 scopus 로고    scopus 로고
    • Catalysis of protein folding by symmetric chaperone complexes
    • Sparrer H., Rutkat K., Buchner J. Catalysis of protein folding by symmetric chaperone complexes. Proc. Natl Acad. Sci. USA. 94:1997;1096-1100.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1096-1100
    • Sparrer, H.1    Rutkat, K.2    Buchner, J.3
  • 22
    • 0038933540 scopus 로고    scopus 로고
    • Catalysis, commitment and encapsulation during GroE-mediated folding
    • Beibinger M., Rutkat K., Buchner J. Catalysis, commitment and encapsulation during GroE-mediated folding. J. Mol. Biol. 289:1999;1075-1092.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1075-1092
    • Beibinger, M.1    Rutkat, K.2    Buchner, J.3
  • 24
    • 0029995319 scopus 로고    scopus 로고
    • Allosteric control by ATP of non-folded protein binding to GroEL
    • Yifrach O., Horovitz A. Allosteric control by ATP of non-folded protein binding to GroEL. J. Mol. Biol. 255:1996;356-361.
    • (1996) J. Mol. Biol. , vol.255 , pp. 356-361
    • Yifrach, O.1    Horovitz, A.2
  • 25
    • 0029823985 scopus 로고    scopus 로고
    • Release of both native and non-native proteins from a cis-only GroEL ternary complex
    • Burston S.G., Weissman J.S., Farr G.W., Fenton W.A., Horwich A.L. Release of both native and non-native proteins from a cis-only GroEL ternary complex. Nature. 383:1996;96-99.
    • (1996) Nature , vol.383 , pp. 96-99
    • Burston, S.G.1    Weissman, J.S.2    Farr, G.W.3    Fenton, W.A.4    Horwich, A.L.5
  • 27
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding-active rings
    • Rye H.S., Roseman A.M., Chen S., Furtak K., Fenton W.A., Saibil H.R., Horwich A.L. GroEL-GroES cycling: ATP and non-native 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    Furtak, K.4    Fenton, W.A.5    Saibil, H.R.6    Horwich, A.L.7
  • 28
    • 0029004759 scopus 로고
    • Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
    • Yifrach O., Horovitz A. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry. 34:1995;5303-5308.
    • (1995) Biochemistry , vol.34 , pp. 5303-5308
    • Yifrach, O.1    Horovitz, A.2
  • 29
    • 0027419011 scopus 로고
    • Binding and hydrolysis of nucleotides in the chaperonie catalytic cycle: Implications for the mechanism of assisted protein folding
    • Jackson G.S., Staniforth R.A., Halsall D.J., Atkinson T., Holbrook J.J., Clarke A.R., Burston S.G. Binding and hydrolysis of nucleotides in the chaperonie catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry. 32:1993;2554-2563.
    • (1993) Biochemistry , vol.32 , pp. 2554-2563
    • Jackson, G.S.1    Staniforth, R.A.2    Halsall, D.J.3    Atkinson, T.4    Holbrook, J.J.5    Clarke, A.R.6    Burston, S.G.7
  • 31
    • 0033569635 scopus 로고    scopus 로고
    • Chaperonin-affected refolding of a-lactalbumin: Effects of nucleotides and the co-chaperonin GroES
    • Makio T., Arai M., Kuwajima K. Chaperonin-affected refolding of a-lactalbumin: effects of nucleotides and the co-chaperonin GroES. J. Mol. Biol. 293:1999;125-137.
    • (1999) J. Mol. Biol. , vol.293 , pp. 125-137
    • Makio, T.1    Arai, M.2    Kuwajima, K.3
  • 32
    • 0031436142 scopus 로고    scopus 로고
    • Calorimetric observation of a GroEL-protein interaction with little contribution of hydrophobic interaction
    • Aoki K., Taguchi H., Shindo Y., Yoshida M., Ogasahara K., Yutani K., Tanaka N. Calorimetric observation of a GroEL-protein interaction with little contribution of hydrophobic interaction. J. Biol. Chem. 272:1997;32158-32162.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32158-32162
    • Aoki, K.1    Taguchi, H.2    Shindo, Y.3    Yoshida, M.4    Ogasahara, K.5    Yutani, K.6    Tanaka, N.7
  • 33
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
    • Braig K., Adams P., Brunger A.T. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nature Struct. Biol. 2:1995;1083-1094.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.2    Brunger, A.T.3
  • 34
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • Stebbins C.E., Galan J.E. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature. 414:2001;77-81.
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 35
    • 0023652256 scopus 로고
    • Molecular structure of a new family of ribonucleases
    • McPhalen C.A., James M.N. Molecular structure of a new family of ribonucleases. Biochemistry. 26:1987;261-269.
    • (1987) Biochemistry , vol.26 , pp. 261-269
    • Mcphalen, C.A.1    James, M.N.2
  • 36
    • 0019944172 scopus 로고
    • Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds
    • Mauguen Y., Hartley R.W., Dodson E.J., Dodson G.G., Bricogne G., Chothia C., Jack A. Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds. Nature. 297:1982;162-164.
    • (1982) Nature , vol.297 , pp. 162-164
    • Mauguen, Y.1    Hartley, R.W.2    Dodson, E.J.3    Dodson, G.G.4    Bricogne, G.5    Chothia, C.6    Jack, A.7
  • 37
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interface
    • Lawrence M.C., Colman P.M. Shape complementarity at protein/protein interface. J. Mol. Biol. 234:1993;946-950.
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 38
    • 18544375930 scopus 로고    scopus 로고
    • Structural plasticity and non-covalent substrate binding in the GroEL apical domain
    • Ashcroft A.E., Brinker A., Coyle J.E., Weber F., Kaiser M., Moroder L., et al. Structural plasticity and non-covalent substrate binding in the GroEL apical domain. J. Biol. Chem. 277:2003;33115-33126.
    • (2003) J. Biol. Chem. , vol.277 , pp. 33115-33126
    • Ashcroft, A.E.1    Brinker, A.2    Coyle, J.E.3    Weber, F.4    Kaiser, M.5    Moroder, L.6
  • 40
    • 0025291463 scopus 로고
    • The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor
    • Laminet A.A., Ziegelhoffer T., Georgopoulos C., Pluckthun A. The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor. EMBO J. 9:1990;2315-2319.
    • (1990) EMBO J. , vol.9 , pp. 2315-2319
    • Laminet, A.A.1    Ziegelhoffer, T.2    Georgopoulos, C.3    Pluckthun, A.4
  • 41
    • 0035913910 scopus 로고    scopus 로고
    • GroEL/GroES-mediated folding of a protein too large to be encapsulated
    • Chaudhuri T.K., Farr G.W., Fenton W.A., Rospert S., Horwich A.L. GroEL/GroES-mediated folding of a protein too large to be encapsulated. Cell. 107:2001;235-246.
    • (2001) Cell , vol.107 , pp. 235-246
    • Chaudhuri, T.K.1    Farr, G.W.2    Fenton, W.A.3    Rospert, S.4    Horwich, A.L.5
  • 42
    • 0037926429 scopus 로고    scopus 로고
    • Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes
    • Farr G.W., Fenton W.A., Chaudhuri T.K., Clare D.K., Saibil H.R., Horwich A.L. Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes. EMBO J. 22:2003;3220-3230.
    • (2003) EMBO J. , vol.22 , pp. 3220-3230
    • Farr, G.W.1    Fenton, W.A.2    Chaudhuri, T.K.3    Clare, D.K.4    Saibil, H.R.5    Horwich, A.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.