Molecular Mechanism of Protein Folding in the Cell

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Molecular Mechanism of Protein Folding in the Cell James E. Rothman, Randy Schekman Cell Volume 146, Issue 6, Pages 851-854 (September 2011) DOI: 10.1016/j.cell.2011.08.041 Copyright © 2011 Elsevier Inc. Terms and Conditions

Figure 1 Chaperone Pathway for the Folding in the E. coli Cytosol The Hsp70 chaperones DnaK/DnaJ stabilize the newly synthesized protein in a nonaggregated, folding-competent state. Transferring the protein into the central cavity of the Hsp60 chaperone GroEL requires the nucleotide exchange factor GrpE. GroES binds to GroEL in an ATP-dependent reaction and displaces the unfolded protein into an enclosed folding cage. The protein is allowed to fold inside the cage for ∼10 s, the time needed for GroEL to complete one round of ATP hydrolysis (of 7 ATPs). Binding of ATP to the opposite ring of GroEL induces an allosteric change that triggers the opening of the folding chamber. Folded protein is released, whereas incompletely folded protein re-binds to GroEL for another round of attempted folding in the GroEL-GroES cage. Cell 2011 146, 851-854DOI: (10.1016/j.cell.2011.08.041) Copyright © 2011 Elsevier Inc. Terms and Conditions