The role of ATP hydrolysis in the function of the chaperonin GroEL: dynamic complex formation with GroES
- 7 August 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 369 (2-3) , 283-286
- https://doi.org/10.1016/0014-5793(95)00768-5
Abstract
In order to understand the role of ATP hydrolysis of the chaperonin GroEL during protein folding, we have studied GroEL‐GroES complex formation in the presence of ATP or ADP by using capillary electrophoresis and surface plasmon resonance. Capillary electrophoresis analysis showed that the GroEL 14‐mer and GroES 7‐mer formed a 1:1 complex in the presence of ATP. In the presence of ADP, both the association and dissociation rates of the complex were slower by about one order of magnitude than the rates in the presence of ATP at 25°C. The implications of such a stable complex on the overall mechanism of chaperonin function are discussed.Keywords
This publication has 30 references indexed in Scilit:
- The Hydrophobic Nature of GroEL-Substrate BindingJournal of Biological Chemistry, 1995
- The guanidine-induced conformational changes of the chaperonin GroEL from Escherichia coli Evidence for the existence of an unfolding intermediate stateBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994
- Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein FoldingScience, 1994
- Chaperonin GroE and ADP facilitate the folding of various proteins and protect against heat inactivationFEBS Letters, 1994
- The formation of symmetrical GroEL‐GroES complexes in the presence of ATPFEBS Letters, 1994
- Assembly and function of a quaternary signal transduction complex monitored by surface plasmon resonanceNature, 1993
- Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein foldingBiochemistry, 1993
- Cooperativity in ATP hydrolysis by GroEL is increased by GroESFEBS Letters, 1991
- Binding of a chaperonin to the folding intermediates of lactate dehydrogenaseBiochemistry, 1991
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976