Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes

Nature Structural and Molecular Biology

Volumn 13, Issue 2, 2006, Pages 147-152

  Ranson, Neil A ^a,b   Clare, Daniel K ^b   Farr, George W ^c   Houldershaw, David ^b   Horwich, Arthur L ^c,d   Saibil, Helen R ^b  

^a UNIVERSITY OF LEEDS   (United Kingdom)

^b UNIVERSITY OF LONDON   (United Kingdom)

^c HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^d SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; NUCLEOTIDE;

ALLOSTERISM; ARTICLE; CONFORMATION; HYDROLYSIS; IMAGE PROCESSING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALLOSTERIC REGULATION; CRYOELECTRON MICROSCOPY; GROEL PROTEIN; GROES PROTEIN; HYDROLYSIS; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY;

EID: 32244441663     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1046     Document Type: Article

References (26)

1. Sigler, P.B. et al. Structure and function in GroEL-mediated protein folding. Annu. Rev. Biochem. 67, 581-608 (1998).
2. Saibil, H.R. & Ranson, N.A. The chaperonin folding machine. Trends Biochem. Sci. 27, 627-632 (2002).
3. Hartl, F.U. & Hayer-Hartl, F.U. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858 (2002).
4. Fenton, W.A. & Norwich, A.L. Chaperone-mediated protein folding: fate of substrate polypeptide. Q. Rev. Biophys. 36, 229-256 (2003).
5. Yifrach, O. & Horovitz, A. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196->Ala. J. Mol. Biol. 243, 397-401 (1994).
6. Yifrach, O. & Horovitz, A. Nested co-operativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry 34, 5303-5308 (1995).
7. Ranson, N.A. et al. ATP bound states of GroEL captured by cryo-electron microscopy. Cell 107, 869-879 (2001).
8. 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).
9. 7 chaperonin complex. Nature 388, 741-750 (1997).
10. Weissman, J.S., Rye, H.S., Fenton, W.A., Beecham, J.M. & Norwich, A.L. Characterisation of the active folding intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 84, 481-490 (1996).
11. Rye, H.S. et al. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 388, 792-798 (1997).
12. Rye, H.S. et al. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding active rings. Cell 97, 325-338 (1999).
13. Chaudhry, C. et al. Role of the γ-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics. EMBO J. 22, 4877-4887 (2003).
14. Navaza, J., Lepault, J., Rey, F.A., Álvarez-Rúa, C. & Borge, J. On the fitting of model electron densities in EM reconstructions: a reciprocal space formulation. Acta Crystallogr. D Biol. Crystallogr. 58, 1820-1825 (2002).
15. Horovitz, A., Bochkareva, E.S., Yifrach, O. & Girshovich, A.S. Prediction of an inter-residue interaction in the chaperonin GroEL from multiple sequence alignment is confirmed by double-mutant cycle analysis. J. Mol. Biol. 238, 133-138 (1994).
16. Braig, K. et al. The crystal structure of the bacterial chaperonin GroEL at 2.SÅ resolution. Nature 371, 578-586 (1994).
17. White, H.E. et al. Structural basis for allosteric changes in the GroEL mutant Arg197→Ala. Nat. Struct. Biol. 4, 690-694 (1997).
18. Vale, R.D. & Milligan, R.A. The way things move: looking under the hood of molecular motor proteins. Science 288, 88-95 (2000).
19. Dubochet, J. Cryo-electron microscopy of vitrified specimens. Q. Rev. Biophys. 21, 129-228 (1988).
20. Mindell, J.A. & Grigorieff, N. Accurate determination of microscope defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
21. Smith, J.M. Ximdisp - A visualization tool to aid structure determination from electron microscope images. J. Struct. Biol. 125, 223-228 (1999).
22. Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199 (1996).
23. Frigo, M. & Johnson, S.G. FFTW: an adaptive software architecture for the FFT. ICASSP Conference Proceedings 3, 1381-1384 (1998).
24. van Heel, M., Harauz, G., Orlova, E.V., Schmidt, R. & Schatz, M. A new generation of the IMAGIC image processing system. J. Struct. Biol. 116, 17-24 (1996).
25. Roseman, A.M., Ranson, N.A., Gowen, B., Fuller, S.D. & Saibil, H.R. The ATP-bound state of the E. coli chaperonin GroEL studied by cryo-electron microscopy. J. Struct. Biol. 135, 115-125 (2001).
26. Case, D.A. et al. The Amber biomolecular simulation programs. J. Comput. Chem. 26, 1668-1688 (2005).