Biochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeast
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 dif...
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| Format: | Book chapter |
| Language: | en_US |
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Elsevier Inc.
2011
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| Online Access: | http://hdl.handle.net/1721.1/66916 https://orcid.org/0000-0003-1307-882X |
| _version_ | 1811072484067246080 |
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| author | Alberti, Simon Halfmann, Randal Arthur Lindquist, Susan |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Alberti, Simon Halfmann, Randal Arthur Lindquist, Susan |
| author_sort | Alberti, Simon |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T09:06:41Z |
| format | Book chapter |
| id | mit-1721.1/66916 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T09:06:41Z |
| publishDate | 2011 |
| publisher | Elsevier Inc. |
| record_format | dspace |
| spelling | mit-1721.1/669162022-09-30T13:28:44Z Biochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeast Alberti, Simon Halfmann, Randal Arthur Lindquist, Susan Massachusetts Institute of Technology. Department of Biology Whitehead Institute for Biomedical Research Lindquist, Susan Alberti, Simon Halfmann, Randal Arthur Lindquist, Susan 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. 2011-11-03T19:07:43Z 2011-11-03T19:07:43Z 2010-01 Book chapter http://purl.org/eprint/type/BookItem 978-0-12-385118-5 http://hdl.handle.net/1721.1/66916 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. https://orcid.org/0000-0003-1307-882X en_US http://dx.doi.org/10.1016/s0076-6879(10)70030-6 Methods in Enzymology Creative Commons Attribution-Noncommercial-Share Alike 3.0 http://creativecommons.org/licenses/by-nc-sa/3.0/ application/pdf Elsevier Inc. Lindquist |
| spellingShingle | Alberti, Simon Halfmann, Randal Arthur Lindquist, Susan Biochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeast |
| title | Biochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeast |
| title_full | Biochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeast |
| title_fullStr | Biochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeast |
| title_full_unstemmed | Biochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeast |
| title_short | Biochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeast |
| title_sort | biochemical cell biological and genetic assays to analyze amyloid and prion aggregation in yeast |
| url | http://hdl.handle.net/1721.1/66916 https://orcid.org/0000-0003-1307-882X |
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