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A hierarchy of protein–protein interactions directs trigger factor (TF) to chaperone and release nascent polypeptides. In the cytosol, TF exists in equilibrium between monomeric and dimeric states. Monomeric TF can interact with ribosomes, but its tighter affinity for translating ribosomes allows TF to selectively chaperone nascent polypeptides. As translation continues, TF can remain bound to the polypeptide and eventually dissociate to repeat the cycle.
