Related Experiment Video
Updated: May 23, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
Published on: June 7, 2020
Ribosome-associated chaperones as key players in proteostasis
Steffen Preissler1, Elke Deuerling
1Molecular Microbiology, Department of Biology, University of Konstanz, 78457 Konstanz, Germany.
Abstract:
De novo protein folding is delicate and error-prone and requires the guidance of molecular chaperones. Besides cytosolic and organelle-specific chaperones, cells have evolved ribosome-associated chaperones that support early folding events and prevent misfolding and aggregation. This class of chaperones includes the bacterial trigger factor (TF), the archaeal and eukaryotic nascent polypeptide-associated complex (NAC) and specialized eukaryotic heat shock protein (Hsp) 70/40 chaperones. This review focuses on the cellular activities of ribosome-associated chaperones and highlights new findings indicating additional functions beyond de novo folding. These activities include the assembly of oligomeric complexes, such as ribosomes, modulation of translation and targeting of proteins.
Related Concept Videos
Bacterial Protein Maturation
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...
Regulation of the Unfolded Protein Response
Export of Misfolded Proteins out of the ER
Post-translational Translocation of Proteins to the RER
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
