Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins

Article

关键词: NEWLY SYNTHESIZED PROTEINS;    ESCHERICHIA-COLI;    PEPTIDE;    DOMAINS;    DNAK;    ISOMERASE;    CYTOSOL;    BINDING;    CHAINS;   

DOI  :  10.1038/nature02899

来源: SCIE

【 摘 要 】

During protein biosynthesis, nascent polypeptide chains that emerge from the ribosomal exit tunnel encounter ribosome-associated chaperones, which assist their folding to the native state(1,2). Here we present a 2.7 Angstrom crystal structure of Escherichia coli trigger factor, the best-characterized chaperone of this type, together with the structure of its ribosome-binding domain in complex with the Haloarcula marismortui large ribosomal subunit. Trigger factor adopts a unique conformation resembling a crouching dragon with separated domains forming the amino-terminal ribosome-binding 'tail', the peptidylprolyl isomerase 'head', the carboxy-terminal 'arms' and connecting regions building up the 'back'. From its attachment point on the ribosome, trigger factor projects the extended domains over the exit of the ribosomal tunnel, creating a protected folding space where nascent polypeptides may be shielded from proteases and aggregation. This study sheds new light on our understanding of co-translational protein folding, and suggests an unexpected mechanism of action for ribosome-associated chaperones.

【 授权许可】

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