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.
Frydman
J
J
Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021.
Nimmesgern
E
E
Ohtsuka
K
K
Hartl
F U
FU
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