NR AVYV

AU Shewmaker,F.; Wickner,R.B.; Tycko,R.

TI Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure

QU Proceedings of the National Academy of Sciences of the United States of America 2006 Dec 26; 103(52): 19754-9

PT journal article; research support, non-u.s. gov't

AB 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 N-terminal 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 approximately 0.5 nm for nearly all sites in the N domain. Certain sites in the M domain also exhibit intermolecular distances of approximately 0.5 nm. These results indicate that an in-register parallel beta-sheet structure underlies the [PSI(+)] prion phenomenon.

MH Amino Acid Sequence; Amyloid/*chemistry/ultrastructure; Carbon Isotopes; Microscopy, Electron, Transmission; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Prions/*chemistry/ultrastructure; Protein Structure, Secondary; Saccharomyces cerevisiae Proteins/*chemistry/ultrastructure; Time Factors

AD Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA

SP englisch

PO USA

EA pdf-Datei und Zusatzinformationen

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