Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins

• The interaction of the chaperone SecB with ribosome-bound polypeptides that are in the process of elongation has been studied using an in vitro protein synthesis system. The binding is characterized by the same properties as those demonstrated for the bin

Nyckelord

ESCHERICHIA-COLI SECB; CHAPERONE SECB; SELECTIVE BINDING; LEADER PEPTIDE; MATURE PORTION; EXPORT; INVITRO; INVIVO; RECOGNITION; LIGAND

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