Prion formation by a yeast GLFG nucleoporin
The self-assembly of proteins into higher order structures is both central to normal biology and a dominant force in disease. Certain glutamine/asparagine (Q/N)-rich proteins in the budding yeast Saccharomyces cerevisiae assemble into self-replicating amyloid-like protein polymers, or prions, that a...
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| Format: | Article |
| Language: | en_US |
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Landes Bioscience
2014
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| Online Access: | http://hdl.handle.net/1721.1/84962 https://orcid.org/0000-0003-1307-882X |
| _version_ | 1826206820284235776 |
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| author | Halfmann, Randal Arthur Wright, Jessica R. Alberti, Simon Lindquist, Susan Rexach, Michael |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Halfmann, Randal Arthur Wright, Jessica R. Alberti, Simon Lindquist, Susan Rexach, Michael |
| author_sort | Halfmann, Randal Arthur |
| collection | MIT |
| description | The self-assembly of proteins into higher order structures is both central to normal biology and a dominant force in disease. Certain glutamine/asparagine (Q/N)-rich proteins in the budding yeast Saccharomyces cerevisiae assemble into self-replicating amyloid-like protein polymers, or prions, that act as genetic elements in an entirely protein-based system of inheritance. The nuclear pore complex (NPC) contains multiple Q/N-rich proteins whose self-assembly has also been proposed to underlie structural and functional properties of the NPC. Here we show that an essential sequence feature of these proteins—repeating GLFG motifs—strongly promotes their self-assembly into amyloids with characteristics of prions. Furthermore, we demonstrate that Nup100 can form bona fide prions, thus establishing a previously undiscovered ability of yeast GLFG nucleoporins to adopt this conformational state in vivo. |
| first_indexed | 2024-09-23T13:39:05Z |
| format | Article |
| id | mit-1721.1/84962 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T13:39:05Z |
| publishDate | 2014 |
| publisher | Landes Bioscience |
| record_format | dspace |
| spelling | mit-1721.1/849622022-10-01T16:15:31Z Prion formation by a yeast GLFG nucleoporin Halfmann, Randal Arthur Wright, Jessica R. Alberti, Simon Lindquist, Susan Rexach, Michael Massachusetts Institute of Technology. Department of Biology Whitehead Institute for Biomedical Research Halfmann, Randal Arthur Alberti, Simon Lindquist, Susan The self-assembly of proteins into higher order structures is both central to normal biology and a dominant force in disease. Certain glutamine/asparagine (Q/N)-rich proteins in the budding yeast Saccharomyces cerevisiae assemble into self-replicating amyloid-like protein polymers, or prions, that act as genetic elements in an entirely protein-based system of inheritance. The nuclear pore complex (NPC) contains multiple Q/N-rich proteins whose self-assembly has also been proposed to underlie structural and functional properties of the NPC. Here we show that an essential sequence feature of these proteins—repeating GLFG motifs—strongly promotes their self-assembly into amyloids with characteristics of prions. Furthermore, we demonstrate that Nup100 can form bona fide prions, thus establishing a previously undiscovered ability of yeast GLFG nucleoporins to adopt this conformational state in vivo. G. Harold and Leila Y. Mathers Foundation National Institutes of Health (U.S.) (grant GM061900) National Institutes of Health (U.S.) (grant GM007520) National Institutes of Health (U.S.) (grant GM25874) National Institutes of Health (U.S.) (Director’s Early Independence Award, DP5-OD009152-01) Howard Hughes Medical Institute (Investigator) University of Texas Southwestern Medical Center at Dallas (Frank and Sara McKnight Fellow) 2014-02-14T18:18:58Z 2014-02-14T18:18:58Z 2012-09 2012-03 Article http://purl.org/eprint/type/JournalArticle 1933-6896 http://hdl.handle.net/1721.1/84962 Halfmann, Randal, Jessica R. Wright, Simon Alberti, Susan Lindquist, and Michael Rexach. “Prion formation by a yeast GLFG nucleoporin.” Prion 6, no. 4 (September 1, 2012): 391-399. https://orcid.org/0000-0003-1307-882X en_US http://dx.doi.org/10.4161/pri.20199 Prion Creative Commons Attribution http://creativecommons.org/licenses/by-nc/3.0/ application/pdf Landes Bioscience Prion |
| spellingShingle | Halfmann, Randal Arthur Wright, Jessica R. Alberti, Simon Lindquist, Susan Rexach, Michael Prion formation by a yeast GLFG nucleoporin |
| title | Prion formation by a yeast GLFG nucleoporin |
| title_full | Prion formation by a yeast GLFG nucleoporin |
| title_fullStr | Prion formation by a yeast GLFG nucleoporin |
| title_full_unstemmed | Prion formation by a yeast GLFG nucleoporin |
| title_short | Prion formation by a yeast GLFG nucleoporin |
| title_sort | prion formation by a yeast glfg nucleoporin |
| url | http://hdl.handle.net/1721.1/84962 https://orcid.org/0000-0003-1307-882X |
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