메뉴 건너뛰기




Volumn 141, Issue 3, 2003, Pages 240-258

Interaction of GroEL and GroEL/GroES complexes with a nonnative subtilisin variant: A small-angle neutron scattering study

Author keywords

Chaperones; Contrast variation; GroEL; GroES; Neutron scattering; Polypeptide substrate binding; Small angle scattering

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CHAPERONIN; MUTANT PROTEIN; SUBTILISIN;

EID: 0037340757     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1047-8477(03)00002-9     Document Type: Article
Times cited : (9)

References (39)
  • 2
    • 0029664944 scopus 로고    scopus 로고
    • The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP γ S
    • Boisvert D.C., Wang J., Otwinowski Z.et al. The 2.4. Å crystal structure of the bacterial chaperonin GroEL complexed with ATP γ S 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
  • 5
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
    • Braig K., Adams P.D., Brunger A.T. Conformational variability in the refined structure of the chaperonin GroEL at 2.8. Å resolution Nat. Struct. Biol. 2:1995;1083-1094.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brunger, A.T.3
  • 6
    • 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
  • 7
    • 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., Burston S.G., Ranson N.A., Clarke A.R., Saibil H.R. 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    Burston, S.G.5    Ranson, N.A.6    Clarke, A.R.7    Saibil, H.R.8
  • 8
    • 0031944833 scopus 로고    scopus 로고
    • Overexpression, purification, and properties of GroES from Escherichia coli
    • Eisenstein E., Reddy P., Fisher M.T. Overexpression, purification, and properties of GroES from Escherichia coli. Methods Enzymol. 290:1998;119-135.
    • (1998) Methods Enzymol. , vol.290 , pp. 119-135
    • Eisenstein, E.1    Reddy, P.2    Fisher, M.T.3
  • 9
    • 0034972451 scopus 로고    scopus 로고
    • Structural changes in GroEL effected by binding a denatured protein substrate
    • Falke S., Fisher M.T., Gogol E.P. Structural changes in GroEL effected by binding a denatured protein substrate. J. Mol. Biol. 308:2001;569-577.
    • (2001) J. Mol. Biol. , vol.308 , pp. 569-577
    • Falke, S.1    Fisher, M.T.2    Gogol, E.P.3
  • 10
    • 0035783260 scopus 로고    scopus 로고
    • Classification and reconstruction of a heterogeneous set of electron microscopic images: A case study of GroEL-substrate complexes
    • Falke S., Fisher M.T., Gogol E.P. Classification and reconstruction of a heterogeneous set of electron microscopic images: a case study of GroEL-substrate complexes. J. Struct. Biol. 133:2001;203-213.
    • (2001) J. Struct. Biol. , vol.133 , pp. 203-213
    • Falke, S.1    Fisher, M.T.2    Gogol, E.P.3
  • 11
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton W.A., Kashl 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    Kashl, Y.2    Furtak, K.3    Horwich, A.L.4
  • 14
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia de la Torre J., Huertas M.L., Carrasco B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78:2000;719-730.
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • Garcia de la Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 15
    • 0542443295 scopus 로고    scopus 로고
    • The 30-meter small angle neutron scattering instruments at the National Institute of Standards and Technology
    • Glinka C.J., Barker J.G., Hammouda B., Krueger S., Moyer J.J., Orts W.J. The 30-meter small angle neutron scattering instruments at the National Institute of Standards and Technology. J. Appl. Cryst. 31:1998;430-445.
    • (1998) J. Appl. Cryst. , vol.31 , pp. 430-445
    • Glinka, C.J.1    Barker, J.G.2    Hammouda, B.3    Krueger, S.4    Moyer, J.J.5    Orts, W.J.6
  • 17
    • 0000933071 scopus 로고
    • Calculation of small-angle scattering profiles using Monte Carlo simulation
    • Hansen S. Calculation of small-angle scattering profiles using Monte Carlo simulation. J. Appl. Cryst. 23:1990;334-346.
    • (1990) J. Appl. Cryst. , vol.23 , pp. 334-346
    • Hansen, S.1
  • 18
    • 0034570519 scopus 로고    scopus 로고
    • Interaction of nonnative polypeptide substrates with the Escherichia coli chaperonin GroEL
    • Schneider C. New Jersey: Humana Press
    • Hartmann W.K., Eisenstein E. Interaction of nonnative polypeptide substrates with the Escherichia coli chaperonin GroEL. Schneider C. Methods in Molecular Biology. vol. 140:2000;97-109 Humana Press, New Jersey.
    • (2000) Methods in Molecular Biology , vol.140 , pp. 97-109
    • Hartmann, W.K.1    Eisenstein, E.2
  • 19
    • 0023845141 scopus 로고
    • Comparison of the crystal and solution structures of calmodulin and troponin C
    • Heidorn D.B., Trewhella J. Comparison of the crystal and solution structures of calmodulin and troponin C. Biochemistry. 27:1988;909-915.
    • (1988) Biochemistry , vol.27 , pp. 909-915
    • Heidorn, D.B.1    Trewhella, J.2
  • 20
    • 0026006843 scopus 로고
    • The role of heat-shock and chaperone proteins in protein folding: Possible molecular mechanisms
    • Hubbard T.I., Sander C. The role of heat-shock and chaperone proteins in protein folding: possible molecular mechanisms. Protein Eng. 4:1991;711-717.
    • (1991) Protein Eng. , vol.4 , pp. 711-717
    • Hubbard, T.I.1    Sander, C.2
  • 21
    • 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., Deisenhofer 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    Deisenhofer, J.5
  • 22
    • 0001339660 scopus 로고
    • The study of biological structures by neutron scattering from solution
    • Jacrot B. The study of biological structures by neutron scattering from solution. Rep. Prog. Phys. 39:1976;911-953.
    • (1976) Rep. Prog. Phys. , vol.39 , pp. 911-953
    • Jacrot, B.1
  • 23
    • 84985698663 scopus 로고
    • Determination of molecular weight by neutron scattering
    • Jacrot B., Zaccai G. Determination of molecular weight by neutron scattering. Biopolymers. 20:1981;2413-2426.
    • (1981) Biopolymers , vol.20 , pp. 2413-2426
    • Jacrot, B.1    Zaccai, G.2
  • 24
    • 0031260295 scopus 로고    scopus 로고
    • Stable expression and rapid purification of Escherichia coli GroEL and GroES chaperonins
    • Kamireddi M., Eisenstein E., Reddy P. Stable expression and rapid purification of Escherichia coli GroEL and GroES chaperonins. Protein Expr. Purif. 11:1997;47-52.
    • (1997) Protein Expr. Purif. , vol.11 , pp. 47-52
    • Kamireddi, M.1    Eisenstein, E.2    Reddy, P.3
  • 25
    • 0029032691 scopus 로고
    • Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering
    • Kataoka M., Nishii I., Fujisawa T., Ueki T., Tokunaga F., Goto Y. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol. 249:1995;215-228.
    • (1995) J. Mol. Biol. , vol.249 , pp. 215-228
    • Kataoka, M.1    Nishii, I.2    Fujisawa, T.3    Ueki, T.4    Tokunaga, F.5    Goto, Y.6
  • 26
    • 0031050429 scopus 로고    scopus 로고
    • Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering
    • Kataoka M., Kuwajima K., Tokunaga F., Goto Y. Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering. Protein Sci. 6:1997;422-430.
    • (1997) Protein Sci. , vol.6 , pp. 422-430
    • Kataoka, M.1    Kuwajima, K.2    Tokunaga, F.3    Goto, Y.4
  • 27
    • 0029875225 scopus 로고    scopus 로고
    • Nucleotide binding-promoted conformational changes release a nonnative polypeptide from the Escherichia coli chaperonin GroEL
    • Lin Z., Eisenstein E. Nucleotide binding-promoted conformational changes release a nonnative polypeptide from the Escherichia coli chaperonin GroEL. Proc. Natl. Acad. Sci. USA. 93:1996;1977-1981.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1977-1981
    • Lin, Z.1    Eisenstein, E.2
  • 28
    • 0027525938 scopus 로고
    • The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable
    • McLennan N.F., Girshovich A.S., Lissin N.M., Charters Y., Masters M. The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable. Mol. Microbiol. 7:1993;49-58.
    • (1993) Mol. Microbiol. , vol.7 , pp. 49-58
    • McLennan, N.F.1    Girshovich, A.S.2    Lissin, N.M.3    Charters, Y.4    Masters, M.5
  • 30
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman A.M., Chen S., White H., Braig K., Saibil H.R. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell. 87:1996;241-251.
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 31
    • 0033597834 scopus 로고    scopus 로고
    • On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES
    • Sakigawa C., Taguchi H., Makino Y., Yoshida M. On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES. J. Biol. Chem. 274:1999;21251-21256.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21251-21256
    • Sakigawa, C.1    Taguchi, H.2    Makino, Y.3    Yoshida, M.4
  • 34
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D., Barberato C., Koch M.H. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Cryst. 28:1995;768-773.
    • (1995) J. Appl. Cryst. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 35
    • 0344035253 scopus 로고
    • Seattle, USA: University of Washington
    • Swanson E. PSSHOW version 19. 1995;University of Washington, Seattle, USA.
    • (1995) PSSHOW version 19
    • Swanson, E.1
  • 36
    • 0029643911 scopus 로고    scopus 로고
    • Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering
    • Thiyagarajan P., Henderson S.J., Joachimiak A. Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering. Structure. 4:1996;79-88.
    • (1996) Structure , vol.4 , pp. 79-88
    • Thiyagarajan, P.1    Henderson, S.J.2    Joachimiak, A.3
  • 37
    • 0029294745 scopus 로고
    • All roads lead to Rome? The multiple pathways of protein folding
    • Weissman I.S. All roads lead to Rome? The multiple pathways of protein folding. Chem. Biol. 2:1995;255-260.
    • (1995) Chem. Biol. , vol.2 , pp. 255-260
    • Weissman, I.S.1
  • 38
    • 0030056969 scopus 로고    scopus 로고
    • Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
    • Weissman J.S., Rye H.S., Fenton W.A., Beechem J.A., Horwich A.L. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell. 84:1996;481-490.
    • (1996) Cell , vol.84 , pp. 481-490
    • Weissman, J.S.1    Rye, H.S.2    Fenton, W.A.3    Beechem, J.A.4    Horwich, A.L.5
  • 39
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.