Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-07

AUTHORS

Judith Frydman, Elmar Nimmesgern, Kenzo Ohtsuka, F. Ulrich Hartl

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. More... »

PAGES

111-117

Journal

TITLE

Nature

ISSUE

6485

VOLUME

370

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/370111a0

DOI

http://dx.doi.org/10.1038/370111a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1002529043

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8022479


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