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Application of yeast to studying amyloid and prion diseases.
Adv Genet. 2020; 105:293-380.AG

Abstract

Amyloids are fibrous cross-β protein aggregates that are capable of proliferation via nucleated polymerization. Amyloid conformation likely represents an ancient protein fold and is linked to various biological or pathological manifestations. Self-perpetuating amyloid-based protein conformers provide a molecular basis for transmissible (infectious or heritable) protein isoforms, termed prions. Amyloids and prions, as well as other types of misfolded aggregated proteins are associated with a variety of devastating mammalian and human diseases, such as Alzheimer's, Parkinson's and Huntington's diseases, transmissible spongiform encephalopathies (TSEs), amyotrophic lateral sclerosis (ALS) and transthyretinopathies. In yeast and fungi, amyloid-based prions control phenotypically detectable heritable traits. Simplicity of cultivation requirements and availability of powerful genetic approaches makes yeast Saccharomyces cerevisiae an excellent model system for studying molecular and cellular mechanisms governing amyloid formation and propagation. Genetic techniques allowing for the expression of mammalian or human amyloidogenic and prionogenic proteins in yeast enable researchers to capitalize on yeast advantages for characterization of the properties of disease-related proteins. Chimeric constructs employing mammalian and human aggregation-prone proteins or domains, fused to fluorophores or to endogenous yeast proteins allow for cytological or phenotypic detection of disease-related protein aggregation in yeast cells. Yeast systems are amenable to high-throughput screening for antagonists of amyloid formation, propagation and/or toxicity. This review summarizes up to date achievements of yeast assays in application to studying mammalian and human disease-related aggregating proteins, and discusses both limitations and further perspectives of yeast-based strategies.

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Authors+Show Affiliations

Chernoff YO
School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA, United States; Laboratory of Amyloid Biology, St. Petersburg State University, St. Petersburg, Russia. Electronic address: yury.chernoff@biology.gatech.edu.
Grizel AV
Laboratory of Amyloid Biology, St. Petersburg State University, St. Petersburg, Russia.
Rubel AA
Laboratory of Amyloid Biology, St. Petersburg State University, St. Petersburg, Russia; Department of Genetics and Biotechnology, St. Petersburg State University, St. Petersburg, Russia; Sirius University of Science and Technology, Sochi, Russia.
Zelinsky AA
Laboratory of Amyloid Biology, St. Petersburg State University, St. Petersburg, Russia.
Chandramowlishwaran P
School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA, United States.
Chernova TA
Department of Biochemistry, Emory University School of Medicine, Atlanta, GA, United States.

MeSH

Alzheimer DiseaseAmyloid beta-PeptidesAmyloidosisAmyotrophic Lateral SclerosisAnimalsHumansParkinson DiseasePrion DiseasesPrionsRecombinant Fusion ProteinsSaccharomyces cerevisiaealpha-Synucleintau Proteins

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

32560789

Citation

Chernoff, Yury O., et al. "Application of Yeast to Studying Amyloid and Prion Diseases." Advances in Genetics, vol. 105, 2020, pp. 293-380.
Chernoff YO, Grizel AV, Rubel AA, et al. Application of yeast to studying amyloid and prion diseases. Adv Genet. 2020;105:293-380.
Chernoff, Y. O., Grizel, A. V., Rubel, A. A., Zelinsky, A. A., Chandramowlishwaran, P., & Chernova, T. A. (2020). Application of yeast to studying amyloid and prion diseases. Advances in Genetics, 105, 293-380. https://doi.org/10.1016/bs.adgen.2020.01.002
Chernoff YO, et al. Application of Yeast to Studying Amyloid and Prion Diseases. Adv Genet. 2020;105:293-380. PubMed PMID: 32560789.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Application of yeast to studying amyloid and prion diseases. AU - Chernoff,Yury O, AU - Grizel,Anastasia V, AU - Rubel,Aleksandr A, AU - Zelinsky,Andrew A, AU - Chandramowlishwaran,Pavithra, AU - Chernova,Tatiana A, Y1 - 2020/05/04/ PY - 2020/6/21/entrez PY - 2020/6/21/pubmed PY - 2021/1/13/medline KW - Alzheimer's disease KW - Amyloid β KW - Amyotrophic lateral sclerosis KW - Huntington's disease KW - Parkinson's disease KW - Prion protein KW - Protein aggregation KW - Tau KW - Transthyretin KW - α-Synuclein SP - 293 EP - 380 JF - Advances in genetics JO - Adv Genet VL - 105 N2 - Amyloids are fibrous cross-β protein aggregates that are capable of proliferation via nucleated polymerization. Amyloid conformation likely represents an ancient protein fold and is linked to various biological or pathological manifestations. Self-perpetuating amyloid-based protein conformers provide a molecular basis for transmissible (infectious or heritable) protein isoforms, termed prions. Amyloids and prions, as well as other types of misfolded aggregated proteins are associated with a variety of devastating mammalian and human diseases, such as Alzheimer's, Parkinson's and Huntington's diseases, transmissible spongiform encephalopathies (TSEs), amyotrophic lateral sclerosis (ALS) and transthyretinopathies. In yeast and fungi, amyloid-based prions control phenotypically detectable heritable traits. Simplicity of cultivation requirements and availability of powerful genetic approaches makes yeast Saccharomyces cerevisiae an excellent model system for studying molecular and cellular mechanisms governing amyloid formation and propagation. Genetic techniques allowing for the expression of mammalian or human amyloidogenic and prionogenic proteins in yeast enable researchers to capitalize on yeast advantages for characterization of the properties of disease-related proteins. Chimeric constructs employing mammalian and human aggregation-prone proteins or domains, fused to fluorophores or to endogenous yeast proteins allow for cytological or phenotypic detection of disease-related protein aggregation in yeast cells. Yeast systems are amenable to high-throughput screening for antagonists of amyloid formation, propagation and/or toxicity. This review summarizes up to date achievements of yeast assays in application to studying mammalian and human disease-related aggregating proteins, and discusses both limitations and further perspectives of yeast-based strategies. SN - 0065-2660 UR - https://www.unboundmedicine.com/medline/citation/32560789/Application_of_yeast_to_studying_amyloid_and_prion_diseases_ DB - PRIME DP - Unbound Medicine ER -