Prion formation by a yeast GLFG nucleoporin
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Lindquist_Prion formation.pdf
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1007.24 KB
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Author(s)
Halfmann, Randal Arthur
Wright, Jessica R.
Alberti, Simon
Lindquist, Susan
Rexach, Michael
Date Issued
September 2012
Journal
Prion
Publisher
Landes Bioscience
Citation
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.
Version
Final published version
Abstract
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.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
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Creative Commons Attribution
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DOI of Published Version
https://doi.org/10.4161/pri.20199
