Abstract
Hsp104 is molecular chaperone in the AAA+ family of ATPases that specializes in the resolubilization and refolding of thermally denatured proteins in yeast. In addition to providing high levels of thermotolerance, Hsp104 plays a pivotal role in the propagation of yeast prions, self-replicating, amyloid-like aggregates that are inherited during mitosis and meiosis. In this review, the structure and function of Hsp104 is discussed, its functional interaction with other molecular chaperones, and a model for disaggregation and refolding is proposed.
Related Books
Bioluminescent Marine Plankton
Sustainable Utilization of Fungi in Agriculture and Industry
Myconanotechnology: Green Chemistry for Sustainable Development
Industrial Applications of Soil Microbes
Biomarkers in Medicine
Environmental Microbiology: Advanced Research and Multidisciplinary Applications
Biopolymers Towards Green and Sustainable Development
Algal Biotechnology for Fuel Applications
The Wax Moth: A Problem or a Solution?
Taurine and the Mitochondrion: Applications in the Pharmacotherapy of Human Diseases
9