NR ALOY
AU Taylor,K.L.; Cheng,N.; Williams,R.W.; Steven,A.C.; Wickner,R.B.
TI Prion domain initiation of amyloid formation in vitro from native Ure2p
QU Science 1999 Feb 26; 283(5406): 1339-43
PT journal article
AB The [URE3] non-Mendelian genetic element of Saccharomyces cerevisiae is an infectious protein (prion) form of Ure2p, a regulator of nitrogen catabolism. Here, synthetic Ure2p1-65 were shown to polymerize to form filaments 40 to 45 angstroms in diameter with more than 60 percent beta sheet. Ure2p1-65 specifically induced full-length native Ure2p to copolymerize under conditions where native Ure2p alone did not polymerize. Like Ure2p in extracts of [URE3] strains, these 180- to 220-angstrom-diameter filaments were protease resistant. The Ure2p1-65-Ure2p cofilaments could seed polymerization of native Ure2p to form thicker, less regular filaments. All filaments stained with Congo Red to produce the green birefringence typical of amyloid. This self-propagating amyloid formation can explain the properties of [URE3].
MH Amyloid/*chemistry/metabolism/ultrastructure; Biopolymers/chemistry; Congo Red/metabolism; Dimerization; Dyes/metabolism; Endopeptidases/metabolism; Fungal Proteins/*chemistry/metabolism/ultrastructure; Heat; Microscopy, Electron; Peptide Fragments/chemistry; Precipitation; Prions/*chemistry/metabolism/ultrastructure; Protein Denaturation; Protein Structure, Secondary
AD Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA
SP englisch
PO USA