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.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6262759 | PMC |
| http://dx.doi.org/10.2174/1389201015666141103021035 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Exposed Hsp70-binding site impacts yeast Sup35 prion disaggregation and propagation.
Proc Natl Acad Sci U S A
December 2024
Laboratory for Protein Conformation Diseases, RIKEN Center for Brain Science, Wako, Saitama 351-0198, Japan.
The dynamic balance between formation and disaggregation of amyloid fibrils is associated with many neurodegenerative diseases. Multiple chaperones interact with and disaggregate amyloid fibrils, which impacts amyloid propagation and cellular phenotypes. However, it remains poorly understood whether and how site-specific binding of chaperones to amyloids facilitates the concerted disaggregation process and modulates physiological consequences in vivo.
View Article and Find Full Text PDF[PSI]-CIC: A Deep-Learning Pipeline for the Annotation of Sectored Saccharomyces cerevisiae Colonies.
Bull Math Biol
December 2024
Department of Applied Mathematics, University of California, Merced, 5200 N Lake Drive, Merced, CA, 95343, USA.
The prion phenotype in yeast manifests as a white, pink, or red color pigment. Experimental manipulations destabilize prion phenotypes, and allow colonies to exhibit (red) sectored phenotypes within otherwise completely white colonies. Further investigation of the size and frequency of sectors that emerge as a result of experimental manipulation is capable of providing critical information on mechanisms of prion curing, but we lack a way to reliably extract this information.
View Article and Find Full Text PDFHeMiTo-dynamics: a characterisation of mammalian prion toxicity using non-dimensionalisation, linear stability and perturbation analyses.
Math Med Biol
November 2024
Mathematical Institute, University of Oxford, Andrew Wiles Building, Woodstock Road, OX2 6GG, Oxfordshire, United Kingdom.
Prion-like proteins play crucial parts in biological processes in organisms ranging from yeast to humans. For instance, many neurodegenerative diseases are believed to be caused by the production of prion-like proteins in neural tissue. As such, understanding the dynamics of prion-like protein production is a vital step toward treating neurodegenerative disease.
View Article and Find Full Text PDF[SNG2], a prion form of Cut4/Apc1, confers non-Mendelian inheritance of heterochromatin silencing defect in fission yeast.
Nucleic Acids Res
December 2024
Institute of Microbial Technology, Sector 39A, Chandigarh 160036, India.
Prions represent epigenetic regulator proteins that can self-propagate their structure and confer their misfolded structure and function on normally folded proteins. Like the mammalian prion PrPSc, prions also occur in fungi. While a few prions, like Swi1, affect gene expression, none are shown to affect heterochromatin structure and function.
View Article and Find Full Text PDFPotential of Marine Sponge Metabolites against Prions: Bromotyrosine Derivatives, a Family of Interest.
Mar Drugs
October 2024
Univ Brest, Inserm, EFS, UMR 1078, GGB, School of Medicine, F-29200 Brest, France.
The screening of 166 extracts from tropical marine organisms (invertebrates, macroalgae) and 3 cyclolipopeptides from microorganisms against yeast prions highlighted the potential of Verongiida sponges to prevent the propagation of prions. We isolated the known compounds purealidin Q (), aplysamine-2 (), pseudoceratinine A (), aerophobin-2 (), aplysamine-1 (), and pseudoceratinine B () for the first time from the Wallisian sponge . We then tested compounds - and sixteen other bromotyrosine and bromophenol derivatives previously isolated from Verongiida sponges against yeast prions, demonstrating the potential of -, , , aplyzanzine C (), purealidin A (), psammaplysenes D () and F (), anomoian F (), and N,N-dimethyldibromotyramine ().
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!