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GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
Assembly of foreign prokaryotic ribulose bisphosphate carboxylases (Rubiscos) in Escherichia coli requires both heat-shock proteins groEL and groES. GroEL is related to a chloroplast protein…
Mechanism of Rubisco: The Carbamate as General Base.
Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding.
A unifying model for chaperonin-facilitated protein folding based on successive rounds of binding and release, and partitioning between committed and kinetically trapped intermediates, is proposed.
The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications.
Kinetic analyses indicated that CO2 reacted with an enzyme group whose pK was distinctly alkaline, indicating that the activation of ribulose-1, 5-biphosphate carboxylane involves the formation of a carbamate.
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded poly-peptides is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli, yeast mitochondria or chloroplasts, together with chaper onin-10 from E coli, and Mg-ATP.
Rubisco: structure, mechanisms, and prospects for improvement
Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase.
- P. Viitanen, G. K. Donaldson, G. Lorimer, T. Lubben, A. Gatenby
- Biology, ChemistryBiochemistry
- 8 October 1991
Binding studies with 35S-labeled DHFR support these conclusions and demonstrate that DHFR competes for a common saturable site with another protein (ribulose-1,5-bisphosphate carboxylase) known to interact with chaperonin 60.
D-Ribulose-1,5-bisphosphate carboxylase-oxygenase. Improved methods for the activation and assay of catalytic activities.
Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent.
- P. Viitanen, T. Lubben, J. Reed, P. Goloubinoff, D. O'Keefe, G. Lorimer
- 19 June 1990
It is proposed that a role of chaper onin 10 is to couple the K(+)-dependent hydrolysis of ATP to the release of the folded monomers of the target protein from chaperonin 60.