Kinetic significance of GroEL14· (GroES7)2 complexes in molecular chaperone activity

Folding and Design

Volumn 1, Issue 4, 1996, Pages 265-273

  Corrales, Fernando J ^a   Fersht, Alan R ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Barnase; Chaperonin; Football; Protein folding

Indexed keywords

ADENINE NUCLEOTIDE; BACILLUS AMYLOLIQUEFACIENS RIBONUCLEASE; CHAPERONIN; RIBONUCLEASE;

ARTICLE; CHEMISTRY; GENETICS; KINETICS; MACROMOLECULE; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS; STEREOISOMERISM;

ADENINE NUCLEOTIDES; GROEL PROTEIN; GROES PROTEIN; KINETICS; MACROMOLECULAR SUBSTANCES; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; RIBONUCLEASES; STEREOISOMERISM;

EID: 0030334841     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(96)00040-5     Document Type: Article

References (27)

1. Ellis, R.J. & Hartl, F.U. (1996). Protein folding in the cell: competing models of chaperonin function. FASEB J. 10, 20-26.
2. Lorimer, G.H. & Todd, M.J. (1996). GroE structures galore. Nat Struct. Biol. 3, 116-121.
3. Braig, K., et al., & Sigler, P.B. (1994). The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature 371, 578-586.
4. Braig, K., Adams, P.D. & Brunger, A.T. (1995). Conformational variabil-ity in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nat. Struct. Biol. 2, 1083-1094.
5. Chandrasekhar, G.N., Tilly, K., Woolford, C., Hendrix, R. & Georgopoulos, C. (1986). Purification and properties of the GroES morphogenetic protein of Escherichia coli. J. Biol. Chem. 261, 12414-12419.
6. Chen, S., et al., & Saibil, H.R. (1994). Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature 371, 261 -264.
7. Saibil, H. (1996). The lid that shapes the pot: structure and function of the chaperonin GroES. Structure 4, 1-4.
8. Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M.K. & Hartl, F.U. (1992). Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356, 683-689.
9. Weissman, J.S., et al., & Horwich, A.L. (1995). Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell 83, 577-587.
10. Mayhew, M., Da Silva, A.C.R., Martin, J., Erdjument-Bromage, H., Temps, P. & Hartl, F.U. (1996). Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature 379, 420-426.
11. 2 chaperonin hetero-oligomer. Science 265, 653-656.
12. Schmidt, M., et al., & Buchner, J. (1994). Symmetric complexes of GroE chaperonins as part of the functional cycle. Science 265, 657-659.
13. 2 heterooligomer. Proc. Natl. Acad. Sci. USA 92, 12021-12025.
14. Llorca, O., Carrascosa, J.L. & Valpuesta, J.M. (1996). Biochemical characterization of symmetric GroEL-GroES complexes. Evidence for a role in protein folding. J. Biol. Chem. 271, 68-76.
15. Engel, A., et al., & Hartl, F.U. (1995). Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes. Science 269, 832-836.
16. Corrales, F.J. & Fersht, A.R. (1996). Towards a mechanism for GroEL-ES chaperone activity: an 'ATPase-gated and -pulsed folding and annealing cage'. Proc. Natl. Acad. Sci. USA, in press.
17. Gray, T.E. & Fersht, A.R. (1993). Refolding of barnase in the presence of GroEL. J. Mol. Biol. 232, 1197-1207.
18. Corrales, F.J. & Fersht, A.R. (1995). The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding. Proc. Natl. Acad. Sci. USA 92, 5326-5330.
19. Zahn, R., Perrett, S., Stenberg, G. & Fersht, A.R. (1996). Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Science 271, 642-645.
20. Matthews, C.K. (1972). Biochemistry of deoxyribonucleic acid-defective amber mutants of bacteriophage T4. J. Biol. Chem. 247, 7430-7438.
21. Matouschek, A., Serrano, L. & Fersht, A.R. (1992). The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by protein engineering procedure. J. Mol. Biol. 224, 819-835.
22. Horovitz, A. & Fersht, A. (1992). Co-operative interactions during protein folding. J. Mol. Biol. 224, 733-740.
23. Weissman, J.S, et al., & Horwich, A.L. (1996). Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 84, 481-490.
24. Loewenthal, R., Sancho, J. & Fersht, A.R. (1991). Fluorescence spectrum of barnase: contributions of three tryptophan residues and a histidine-related pH-dependence. Biochemistry 30, 6775-6779.
25. Serrano, L., Horovitz, A., Avron, B., Bycroft, M. & Fersht, A.R. (1990). Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. Biochemistry 29, 9343-9352.
26. Gill, S.C. & Von Hippel, P.H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Analyt. Biochem. 182, 319-326.
27. Bradford, M.M. (1976). A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Analyt. Biochem. 72, 248-254.