Hydrolysable ATP is a requirement for the correct interaction of molecular chaperonins cpn60 and cpn10
- 15 June 2002
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 364 (3) , 849-855
- https://doi.org/10.1042/bj20011643
Abstract
Over recent years the binding ability of the molecular chaperone cpn60 (GroEL14) and its co-chaperone cpn10 (GroES7) has been reported to occur under an assortment of specific conditions from the use of non-hydrolysable ATP analogues (namely adenosine 5'-[gamma-thio]triphosphate) to requiring hydrolysable ATP for any interaction to occur. We have investigated this further using the molecular hydrodynamic methods (hydrodynamic bead modelling, sedimentation-velocity analytical ultracentrifugation and dynamic light-scattering), allowing the process to be followed under physiologically relevant dilute solution conditions, combined with absorption spectrophotometry to determine GroES7-GroEL14 interaction through the rate inhibition of the cpn60's ATPase activity by GroES7. The results found here indicate that the presence of hydrolysable ATP is required to facilitate correct GroES7 interaction with GroEL14 in solution.Keywords
This publication has 22 references indexed in Scilit:
- A Method for Directly Fitting the Time Derivative of Sedimentation Velocity Data and an Alternative Algorithm for Calculating Sedimentation Coefficient Distribution FunctionsAnalytical Biochemistry, 2000
- ATP Binding Induces Large Conformational Changes in the Apical and Equatorial Domains of the Eukaryotic Chaperonin Containing TCP-1 ComplexJournal of Biological Chemistry, 1998
- The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complexNature, 1997
- SOLPRO: theory and computer program for the prediction of SOLution PROperties of rigid macromolecules and bioparticlesEuropean Biophysics Journal, 1997
- Nucleotide-Dependent Complex Formation between the Escherichia coli Chaperonins GroEL and GroES Studied under Equilibrium ConditionsBiochemistry, 1997
- The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.Proceedings of the National Academy of Sciences, 1995
- In vitro dissociation and self‐assembly of three chaperonin 60s: the role of ATPFEBS Letters, 1995
- ATP induces large quaternary rearrangements in a cage-like chaperonin structureCurrent Biology, 1993
- Homologous plant and bacterial proteins chaperone oligomeric protein assemblyNature, 1988
- Purification and properties of the groES morphogenetic protein of Escherichia coli.Journal of Biological Chemistry, 1986