Cooperativity in ATP hydrolysis by GroEL is increased by GroES
- 4 November 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 292 (1-2), 254-258
- https://doi.org/10.1016/0014-5793(91)80878-7
Abstract
The kinetics of ATP hydrolysis by the 'molecular chaperone' GroEL and the inhibition of this hydrolysis by GroES have been studied in more detail. It is shown that the hydrolysis of ATP by GroEL is cooperative with respect to ATP with a Hill coefficient of 1.86 (+/- 0.13). In the presence of GroES, there is an increase in the degree of cooperativity with a Hill coefficient of 3.01 (+/- 0.18). The observed cooperativity is not due to dissociation of the GroEL oligomer into smaller units but more probably involves structural changes within the GroEL oligomer.Keywords
This publication has 22 references indexed in Scilit:
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- (Mg–ATP)-dependent self-assembly of molecular chaperone GroELNature, 1990
- Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATPNature, 1989
- Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cellsCell, 1989
- Molecular chaperones: proteins essential for the biogenesis of some macromolecular structuresTrends in Biochemical Sciences, 1989
- GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coliNature, 1989
- Purification and properties of groE, a host protein involved in bacteriophage assemblyJournal of Molecular Biology, 1979
- Isolation and characterization of the host protein groE involved in bacteriophage lambda assemblyJournal of Molecular Biology, 1979
- Extensions of the Allosteric Model for HaemoglobinNature, 1971
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965