Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones.
basic_science · Level V
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Abstract
The folding of polypeptides emerging from ribosomes was analysed in a mammalian translation system using firefly luciferase as a model protein. The growing polypeptide interacts with a specific set of molecular chaperones, including Hsp70, the DnaJ homologue Hsp40 and the chaperonin TRiC. The ordered assembly of these components on the nascent chain forms a high molecular mass complex that allows the cotranslational formation of protein domains and the completion of folding once the chain is released from the ribosome.
Medical subject headings
- Heat-Shock Proteins
- Intracellular Signaling Peptides and Proteins
- Microtubule-Associated Proteins
- Nuclear Proteins
- Peptide Chain Elongation, Translational
- Protein Folding