FEBS Letters · 1996 · 11 citations · 30 references
Life SciencesBiochemistryMolecular BiologyEnzyme MechanismEnzymologyStructural BiologyEnzyme BiophysicsEnzyme CharacterizationEnzyme FunctionEnzyme KineticsEnzyme-substrate RecognitionMolecular ChaperonesChaperone MutationsChaperone-substrate InteractionsCitrate SynthaseDissociation EquilibriaDissociation EquilibriumEquilibrium Binding ConstantEquilibrium Dissociation ConstantPoint Mutations
Six single point mutants of yeast citrate synthase were analyzed for binding to the molecular chaperone GroEL. In contrast to the wild-type and G276S, all other G276-mutants were able to displace pre-beta-lactamase from GroEL. The off-rate constant for pre-beta-lactamase must be at least partially rate-limiting, leading to an equilibrium dissociation constant between 10(-10) M and 10(-12)M. Direct evidence for binding of citrate synthase was obtained from gel filtration experiments. The results suggest that thermodynamic rather than structural features of the mutants determine the degree of binding to the chaperone.
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The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
K. Braig, Zbyszek Otwinowski, Rashmi S. Hegde et al. · Nature · 1994 · 1.3K citations
Residues in chaperonin GroEL required for polypeptide binding and release
Wayne A. Fenton, Yechezkel Kashi, Krystyna Furtak et al. · Nature · 1994 · 642 citations