酵母在淀粉样蛋白和朊病毒疾病研究中的应用。

4区 生物学 Q2 Biochemistry, Genetics and Molecular Biology
Advances in Genetics Pub Date : 2020-01-01 Epub Date: 2020-05-04 DOI:10.1016/bs.adgen.2020.01.002
Yury O Chernoff, Anastasia V Grizel, Aleksandr A Rubel, Andrew A Zelinsky, Pavithra Chandramowlishwaran, Tatiana A Chernova
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引用次数: 13

摘要

淀粉样蛋白是纤维状的交叉β蛋白聚集体,能够通过有核聚合增殖。淀粉样蛋白构象可能代表一种古老的蛋白质折叠,并与各种生物或病理表现有关。自我延续的淀粉样蛋白构象为称为朊病毒的可传播(感染性或遗传性)蛋白同种异构体提供了分子基础。淀粉样蛋白和朊病毒以及其他类型的错误折叠聚集蛋白与多种破坏性哺乳动物和人类疾病有关,如阿尔茨海默病、帕金森病和亨廷顿病、传染性海绵状脑病(tse)、肌萎缩性侧索硬化症(ALS)和甲状腺变性视网膜病变。在酵母和真菌中,基于淀粉样蛋白的朊病毒控制表型可检测的遗传性状。简单的培养要求和有效的遗传方法使酿酒酵母成为研究淀粉样蛋白形成和繁殖的分子和细胞机制的优秀模型系统。遗传技术允许在酵母中表达哺乳动物或人类淀粉样蛋白和朊原蛋白,使研究人员能够利用酵母的优势来表征疾病相关蛋白的特性。嵌合构建采用哺乳动物和人类聚集倾向蛋白或结构域,融合到荧光团或内源性酵母蛋白中,允许对酵母细胞中疾病相关蛋白聚集进行细胞学或表型检测。酵母系统适用于淀粉样蛋白形成、繁殖和/或毒性拮抗剂的高通量筛选。本文综述了酵母检测在哺乳动物和人类疾病相关聚集蛋白研究中的最新进展,并讨论了基于酵母的检测策略的局限性和进一步的展望。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Application of yeast to studying amyloid and prion diseases.

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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来源期刊
Advances in Genetics
Advances in Genetics 生物-遗传学
CiteScore
5.70
自引率
0.00%
发文量
1
审稿时长
1 months
期刊介绍: Advances in Genetics presents an eclectic mix of articles of use to all human and molecular geneticists. They are written and edited by recognized leaders in the field and make this an essential series of books for anyone in the genetics field.
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