Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones.
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.
Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021.
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Frydman
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Nimmesgern
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Ohtsuka
F U
FU
Hartl
D000255:Adenosine Triphosphate / Q000502:physiology; D000818:Animals; D003600:Cytosol / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000502:physiology*; D066298:In Vitro Techniques; D047908:Intracellular Signaling Peptides and Proteins; D008156:Luciferases / Q000378:metabolism; D008869:Microtubule-Associated Proteins; D008970:Molecular Weight; D009687:Nuclear Proteins / Q000502:physiology*; D010441:Peptide Chain Elongation, Translational / Q000502:physiology*; D014176:Protein Biosynthesis / Q000502:physiology; D017510:Protein Folding; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases; D056427:t-Complex Genome Region
D006360:Heat-Shock Proteins; D047908:Intracellular Signaling Peptides and Proteins; D008869:Microtubule-Associated Proteins; D009687:Nuclear Proteins; D000255:Adenosine Triphosphate; D008156:Luciferases; C116196:PPP1R11 protein, human; D044767:Ubiquitin-Protein Ligases