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 FoundationNational 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
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