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- W2095095972 abstract "The [PSI+] prion is a self-propagating amyloid of the Sup35 protein, normally a subunit of the translation termination factor, but impaired in this vital function when in the amyloid form. The Sup35 N, M, and C domains are the amino-terminal prion domain, a connecting polar domain, and the essential C-terminal domain resembling eukaryotic elongation factor 1α respectively. Different [PSI+] isolates (prion variants) may have distinct biological properties, associated with different amyloid structures. Here we use solid state NMR to examine the structure of infectious Sup35NM amyloid fibrils of two prion variants. We find that both variants have an in-register parallel β-sheet structure, both in the fully hydrated form and in the lyophilized form. Moreover, we confirm that some leucine residues in the M domain participate in the in-register parallel β-sheet structure. Transmission of the [PSI+] prion by amyloid fibrils of Sup35NM and transmission of the [URE3] prion by amyloid fibrils of recombinant full-length Ure2p are similar whether they have been lyophilized or not (wet or dry)." @default.
- W2095095972 created "2016-06-24" @default.
- W2095095972 creator A5011026810 @default.
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- W2095095972 creator A5067483347 @default.
- W2095095972 creator A5068072238 @default.
- W2095095972 date "2009-05-19" @default.
- W2095095972 modified "2023-09-27" @default.
- W2095095972 title "Two Prion Variants of Sup35p Have In-Register Parallel β-Sheet Structures, Independent of Hydration" @default.
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- W2095095972 doi "https://doi.org/10.1021/bi900345q" @default.
- W2095095972 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2744896" @default.
- W2095095972 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19408895" @default.
- W2095095972 hasPublicationYear "2009" @default.
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