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Amyloid of the Prion Domain of Sup35p Has an In-Register Parallel β-Sheet Structure

Frank Shewmaker, Reed B. Wickner and Robert Tycko
Proceedings of the National Academy of Sciences of the United States of America
Vol. 103, No. 52 (Dec. 26, 2006), pp. 19754-19759
Stable URL: http://www.jstor.org/stable/30051383
Page Count: 6
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Amyloid of the Prion Domain of Sup35p Has an In-Register Parallel β-Sheet Structure
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Abstract

The [PSI⁺] prion of Saccharomyces cerevisiae is a self-propagating amyloid form of Sup35p, a subunit of the translation termination factor. Using solid-state NMR we have examined the structure of amyloid fibrils formed in vitro from purified recombinant $Sup35^{1-253}$, consisting of the glutamine- and asparagine-rich Nterminal 123-residue prion domain (N) and the adjacent 130-residue highly charged M domain. Measurements of magnetic dipole-dipole couplings among $^{13}C$ nuclei in a series of Sup35NM fibril samples, $^{13}C-labeled$ at backbone carbonyl sites of Tyr, Leu, or Phe residues or at side-chain methyl sites of Ala residues, indicate intermolecular $^{13}C-^{13}C$ distances of ≈0.5 nm for nearly all sites in the N domain. Certain sites in the M domain also exhibit intermolecular distances of ≈0.5 nm. These results indicate that an in-register parallel β-sheet structure underlies the [PSI⁺] prion phenomenon.

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