| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 268, Issue 29, 21632-21636, Oct, 1993
JE Hansen and A Gafni
Facilitation of protein folding by GroEL usually requires involvement of
GroES and ATP. In their absence nascent proteins tend to be arrested on
GroEL or, if released, fail to show enhancement of reactivation yield
relative to that observed without the chaperonin. In contrast, the yield of
reactivation of glucose-6-phosphate dehydrogenase (Glu-6- PDH) from
Leuconostoc mesenteroides at 20 degrees C is increased 2-3- fold (to over
80%) by GroEL alone. ATP greatly enhances the rate of GroEL-assisted
reactivation and slightly increases its yield to 90%. The efficiency of the
GroEL-assisted reactivation of Glu-6-PDH is strongly dependent on
temperature. A switch from enhanced to fully arrested reactivation occurs
over a narrow temperature range from 25 to 30 degrees C in the presence of
GroEL when ATP is absent. At physiological temperature therefore,
reactivation is fully arrested by GroEL if ATP is absent and in its
presence the protein is released in a form not committed to correct
folding. The data shows that the committing step in Glu-6-PDH refolding
occurs while the nascent protein is bound to GroEL, a step which is
temperature-sensitive. The extreme temperature sensitivity of this step
indicates a sharp structural transition in GroEL.
Thermal switching between enhanced and arrested reactivation of bacterial glucose-6-phosphate dehydrogenase assisted by GroEL in the absence of ATP
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109-2007.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  J. R. Shearstone and F. Baneyx Biochemical Characterization of the Small Heat Shock Protein IbpB from Escherichia coli J. Biol. Chem., April 9, 1999; 274(15): 9937 - 9945. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. P. Ben-Zvi, J. Chatellier, A. R. Fersht, and P. Goloubinoff Minimal and optimal mechanisms for GroE-mediated protein folding PNAS, December 22, 1998; 95(26): 15275 - 15280. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. A. Mendoza and G. D. Campo Ligand-induced Conformational Changes of GroEL Are Dependent on the Bound Substrate Polypeptide J. Biol. Chem., July 5, 1996; 271(27): 16344 - 16349. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. L. Gibbons and D. L. Gibbons Exposure of Hydrophobic Surfaces on the Chaperonin GroEL Oligomer by Protonation or Modification of His-401 J. Biol. Chem., March 31, 1995; 270(13): 7335 - 7340. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Z. Lin, F. P. Schwarz, and E. Eisenstein The Hydrophobic Nature of GroEL-Substrate Binding J. Biol. Chem., January 20, 1995; 270(3): 1011 - 1014. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. R. Mattingly Jr., A. Iriarte, and M. Martinez-Carrion Homologous Proteins with Different Affinities for groEL J. Biol. Chem., January 20, 1995; 270(3): 1138 - 1148. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. Hammarstrom, M. Persson, and U. Carlsson Protein Compactness Measured by Fluorescence Resonance Energy Transfer. HUMAN CARBONIC ANHYDRASE II IS CONSIDERABLY EXPANDED BY THE INTERACTION OF GroEL J. Biol. Chem., June 8, 2001; 276(24): 21765 - 21775. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Li, S. Zhang, and C.-c. Wang Effects of Macromolecular Crowding on the Refolding of Glucose- 6-phosphate Dehydrogenase and Protein Disulfide Isomerase J. Biol. Chem., September 7, 2001; 276(37): 34396 - 34401. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
