Biochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeast
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Alberti2009AssaysGuideYeast.pdf
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1.13 MB
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Adobe PDF
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48a29d386ff4d13fbfb79cdd8fb60834
Author(s)
Alberti, Simon
Halfmann, Randal Arthur
Lindquist, Susan
Date Issued
January 2010
Journal
Methods in Enzymology
Publisher
Elsevier Inc.
Citation
Alberti, Simon, Randal Halfmann, and Susan Lindquist. “Biochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeast.” Methods in Enzymology. Vol. 470. Elsevier, 2010. 709-734. Web. 3 Nov. 2011. © 2011 Elsevier Inc.
Version
Author's final manuscript
Abstract
Protein aggregates are associated with a variety of debilitating human diseases, but they can have functional roles as well. Both pathological and nonpathological protein aggregates display tremendous diversity, with substantial differences in aggregate size, morphology, and structure. Among the different aggregation types, amyloids are particularly remarkable, because of their high degree of order and their ability to form self-perpetuating conformational states. Amyloids form the structural basis for a group of proteins called prions, which have the ability to generate new phenotypes by a simple switch in protein conformation that does not involve changes in the sequence of the DNA. Although protein aggregates are notoriously difficult to study, recent technological developments and, in particular, the use of yeast prions as model systems, have been very instrumental in understanding fundamental aspects of aggregation. Here, we provide a range of biochemical, cell biological and yeast genetic methods that are currently used in our laboratory to study protein aggregation and the formation of amyloids and prions.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
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Creative Commons Attribution-Noncommercial-Share Alike 3.0
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DOI of Published Version
https://doi.org/10.1016/s0076-6879(10)70030-6
