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