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      Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones.

      Nature

      physiology, Animals, Cytosol, metabolism, Heat-Shock Proteins, In Vitro Techniques, Intracellular Signaling Peptides and Proteins, Luciferases, Microtubule-Associated Proteins, Molecular Weight, Nuclear Proteins, t-Complex Genome Region, Peptide Chain Elongation, Translational, Protein Biosynthesis, Protein Folding, Rabbits, Reticulocytes, Ribosomes, Adenosine Triphosphate

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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.

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          Journal
          8022479
          10.1038/370111a0

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