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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphate / physiology
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Animals
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Cytosol / metabolism
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Heat-Shock Proteins / physiology*
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In Vitro Techniques
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Intracellular Signaling Peptides and Proteins*
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Luciferases / metabolism
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Microtubule-Associated Proteins*
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Molecular Weight
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Nuclear Proteins / physiology*
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Peptide Chain Elongation, Translational / physiology*
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Protein Biosynthesis / physiology
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Protein Folding*
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Rabbits
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Reticulocytes / metabolism
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Ribosomes / metabolism
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Ubiquitin-Protein Ligases
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t-Complex Genome Region
Substances
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Heat-Shock Proteins
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Intracellular Signaling Peptides and Proteins
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Microtubule-Associated Proteins
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Nuclear Proteins
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Adenosine Triphosphate
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Luciferases
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PPP1R11 protein, human
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Ubiquitin-Protein Ligases