Related Experiment Video
Updated: Oct 31, 2025

Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models
Published on: November 11, 2014
Ectopic BH3-only protein Bim acts as a cochaperone to positively regulate Hsp70 in yeast
Hao Pan1, Ting Song1, Ziqian Wang1
1State Key Laboratory of Fine Chemicals, School of Chemistry, Dalian University of Technology, Dalian 116012, China.
Abstract:
The chaperone heat shock protein 70 (Hsp70) is conserved from bacteria to humans and is crucial for avoiding protein misfolding under stress. Bim functions, mainly as one of the B-cell lymphoma 2 (Bcl-2) family proapoptotic members, were identified to be a cochaperone of Hsp70. Herein, we reported that ectopic Bim could constitute the interactions with intrinsic Hsp70 and translate its positive cochaperone activity in vitro to the yeast growth promotion and help Hsp70 to fold its client Ras-like protein. With the help of a specific Hsp70/Bim disruptor, we illustrated that Hsp70/Bim dimers rescue yeast from heat shock. In an organism lacks apoptotic Bcl-2 factors, the proapoptotic Bim in mammalian cells exhibits prosurvival functions.
More Related Videos
08:58In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
Published on: September 2, 2019
09:22Budding Yeast Protein Extraction and Purification for the Study of Function, Interactions, and Post-translational Modifications
Published on: October 30, 2013
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
Bacterial Protein Maturation
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...
Regulation of the Unfolded Protein Response