Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

Nature

Volumn 388, Issue 6644, 1997, Pages 792-798

  Rye, Hays S ^a,b   Burston, Steven G ^b   Fenton, Wayne A ^b   Beechem, Joseph M ^c   Xu, Zhaohui ^a   Sigler, Paul B ^a   Horwich, Arthur L ^a,b  

^a YALE UNIVERSITY   (United States)

^b YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; THIOSULFATE SULFURTRANSFERASE;

ARTICLE; CIS TRANS ISOMERISM; COMPLEX FORMATION; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; RHODOSPIRILLUM RUBRUM;

ADENOSINE TRIPHOSPHATE; ADENYLYL IMIDODIPHOSPHATE; ANIMALS; ESCHERICHIA COLI; GROEL PROTEIN; GROES PROTEIN; HYDROLYSIS; MALATE DEHYDROGENASE; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; RHODOSPIRILLUM RUBRUM; RIBULOSE-BISPHOSPHATE CARBOXYLASE; SWINE;

RHODOSPIRILLUM RUBRUM;

EID: 0030804446     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/42047     Document Type: Article

References (24)

1. Weissman, J. S. et al. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell 83, 577-588 (1995).
2. Weissman, J. S., Rye, H. S., Fenton, W. A., Beechem, J. M. & Horwich, A. L. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 84, 481-490 (1996).
3. Mayhew, M. et al. Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature 379, 420-426 (1996).
4. Chandrasekhar, G. N., Tilly, K., Woolford, C., Hendrix, R. & Georgopoulos, C. Purification and properties of the GroES morphogenetic protein of Escherichia coli. J. Biol. Chem. 261, 12414-12419 (1986).
5. Jackson, G. S. et al. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry 32, 2554-2563 (1993).
6. Todd, M. J., Viitanen, P. & Lorimer, G. H. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science 265, 659-666 (1994).
7. Burston, S. G., Ranson, N. A. & Clarke, A. R. The origins and consequences of asymmetry in the chaperonin reaction cycle. J. Mol. Biol. 249, 138-152 (1995).
8. Hayer-Hartl, M., Martin, J. & Hartl, F.-U. Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding. Science 269, 836-841 (1995).
9. Hayer-Hartl, M. K., Weber, F. & Hartl, F.-U. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. EMBO J. 15, 6111-6121 (1996).
10. Goloubinoff, P., Christeller, J. T., Gatenby, A. A. & Lorimer, G. H. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature 342, 884-889 (1989).
11. 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, 4030-4035 (1996).
12. Ranson, N. A., Dunster, N. J., Burston, S. G. & Clarke, A. R. Chaperonins can catalyze the reversal of early aggregation steps when a protein misfolds. J. Mol. Biol. 250, 581-586 (1995).
13. Peralta, D., Hartman, D. J., Hoogenraad, N. J. & Hoj, P. B. Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES. FEBS Lett. 339, 45-49 (1994).
14. Ranson, N. A., Burston, S. G. & Clarke, A. R. Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction. J. Mol. Biol. 266, 656-664 (1997).
15. Weissman, J. S., Kashi, Y., Fenton, W. A. & Horwich, A. L. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell 78, 693-702 (1994).
16. Otto, M, R., Lillo, M. P. & Beechem, J. M. Resolution of multiphasic reactions by the combination of fluorescence total-intensity and anisotropy stopped-flow kinetic experiments. Biophys. J. 67, 2511-2521 (1994).
17. Beechem, J. M., Sherman, M. A. & Mas, M. T. Sequential domain unfolding in phosphoglycerate kinase: fluorescence intensity and anisotropy stopped-flow kinetics of several tryptophan mutants. Biochemistry 34, 13943-13948 (1995).
18. Etfink, M. R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66, 482-501 (1994).
19. 7 chaperonin complex. Nature 388, 741-750 (1997).
20. 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, 241-251 (1996).
21. 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, 96-99 (1996).
22. Pierce, J. & Reddy, G. S. The sites for catalysis and activation of ribulosebisphosphate carboxylase share a common domain. Arch. Biochem. Biophys. 245, 483-493 (1986).
23. Hartl, F. U. Molecular chaperones in cellular protein folding. Nature 381, 571-579 (1996).
24. Fenton, W. A. & Horwich, A. L. GroEL-mediated protein folding. Protein Sci 6, 743-760 (1997).