Related Experiment Video
Updated: Apr 21, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
Published on: August 8, 2017
Yeast prions help identify and define chaperone interaction networks
Michael Reidy, Daniel C Masison1
1Building 8, Room 225, 8 Center Drive, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. reidym@mail.nih.gov.
Abstract:
Proteins in the cell experience various stressful conditions that can affect their ability to attain and maintain the structural conformations they need to perform effectively. Protein chaperones are an important part of a cellular protein quality control system that protects the integrity of the proteome in the face of such challenges. Chaperones from different conserved families have multiple members that cooperate to regulate each other's activity and produce machines that perform a variety of tasks. The large numbers of related chaperones with both functionally overlapping and distinct activities allows fine-tuning of the machinery for specific tasks, but presents a daunting degree of complexity. Yeast prions are misfolded forms of cellular proteins whose propagation depends on the action of protein chaperones. Studying how propagation of yeast prions is affected by alterations in functions of various chaperones provides an approach to understanding this complexity.
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
Yeast Signaling
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Bacterial Protein Maturation
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...

