Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
10.1038/42047
Crossref journal-article
Springer Science and Business Media LLC
Nature (297)
Bibliography

Rye, H. S., Burston, S. G., Fenton, W. A., Beechem, J. M., Xu, Z., Sigler, P. B., & Horwich, A. L. (1997). Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature, 388(6644), 792–798.

Authors 7
  1. Hays S. Rye (first)
  2. Steven G. Burston (additional)
  3. Wayne A. Fenton (additional)
  4. Joseph M. Beechem (additional)
  5. Zhaohui Xu (additional)
  6. Paul B. Sigler (additional)
  7. Arthur L. Horwich (additional)
References 24 Referenced 348
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  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). (10.1016/S0092-8674(00)81293-3) / Cell by JS Weissman (1996)
  3. Mayhew, M.et al. Protein folding in the central cavity of the GroEL–GroES chaperonin complex. Nature 379, 420–426 (1996). (10.1038/379420a0) / Nature by M Mayhew (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). (10.1016/S0021-9258(18)67256-4) / J. Biol. Chem. by GN Chandrasekhar (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). (10.1021/bi00061a013) / Biochemistry by GS Jackson (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). (10.1126/science.7913555) / Science by MJ Todd (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). (10.1006/jmbi.1995.0285) / J. Mol. Biol. by SG Burston (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). (10.1126/science.7638601) / Science by M Hayer-Hartl (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). (10.1002/j.1460-2075.1996.tb00999.x) / EMBO J. by MK Hayer-Hartl (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). (10.1038/342884a0) / Nature by P Goloubinoff (1989)
  11. Todd, M. J., Lorimer, G. H. & Thirumalai, D. Chaperonin-facilitated protein folding: Optimization ofrate and yield by an iterative annealing mechanism. Proc. Natl Acad. Sci. USA 93, 4030–4035 (1996). (10.1073/pnas.93.9.4030) / Proc. Natl Acad. Sci. USA by MJ Todd (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). (10.1006/jmbi.1995.0399) / J. Mol. Biol. by NA Ranson (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). (10.1016/0014-5793(94)80381-1) / FEBS Lett. by D Peralta (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). (10.1006/jmbi.1996.0815) / J. Mol. Biol. by NA Ranson (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). (10.1016/0092-8674(94)90533-9) / Cell by JS Weissman (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). (10.1016/S0006-3495(94)80741-6) / Biophys. J. by MR Otto (1994)
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  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). (10.1038/383096a0) / Nature by SG Burston (1996)
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Dates
Type When
Created 23 years ago (July 26, 2002, 4:37 a.m.)
Deposited 1 year, 5 months ago (Feb. 26, 2024, 1:13 p.m.)
Indexed 1 month, 1 week ago (July 11, 2025, 6:38 a.m.)
Issued 28 years ago (Aug. 21, 1997)
Published 28 years ago (Aug. 21, 1997)
Published Print 28 years ago (Aug. 21, 1997)
Funders 0

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@article{Rye_1997, title={Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL}, volume={388}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/42047}, DOI={10.1038/42047}, number={6644}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Rye, Hays S. and Burston, Steven G. and Fenton, Wayne A. and Beechem, Joseph M. and Xu, Zhaohui and Sigler, Paul B. and Horwich, Arthur L.}, year={1997}, month=aug, pages={792–798} }