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Molecular Mechanism of Protein Folding in the Cell

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Presentation on theme: "Molecular Mechanism of Protein Folding in the Cell"— Presentation transcript:

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

2 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  , DOI: ( /j.cell ) Copyright © 2011 Elsevier Inc. Terms and Conditions

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