NR AHYY
AU Masison,D.C.; Wickner,R.B.
TI Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells
QU Science 1995 Oct 6; 270(5233): 93-5
PT journal article
AB The genetic properties of the [URE3] non-Mendelian element of Saccharomyces cerevisiae suggest that it is a prion (infectious protein) form of Ure2p, a regulator of nitrogen catabolism. In extracts from [URE3] strains, Ure2p was partially resistant to proteinase K compared with Ure2p from wild-type extracts. Overexpression of Ure2p in wild-type strains induced a 20- to 200-fold increase in the frequency with which [URE3] arose. Overexpression of just the amino-terminal 65 residues of Ure2p increased the frequency of [URE3] induction 6000-fold. Without this "prion-inducing domain" the carboxyl-terminal domain performed the nitrogen regulation function of Ure2p, but could not be changed to the [URE3] prion state. Thus, this domain induced the prion state in trans, whereas in cis it conferred susceptibility of the adjoining nitrogen regulatory domain to prion infections.
ZR 26
MH Amino Acid Sequence; Base Sequence; Endopeptidase K; Fungal Proteins/chemistry/*genetics/metabolism; Genes, Fungal; Genetic Complementation Test; Molecular Sequence Data; Nitrogen/metabolism; Plasmids; Prions/*genetics/metabolism; Promoter Regions (Genetics); Saccharomyces cerevisiae/chemistry/*genetics/metabolism; Sequence Deletion; Serine Endopeptidases/metabolism
AD R.B. Wickner, Biochem Pharmacol Lab, Section on Genetics of Simple Eukaryotes, National Institute of Diabetes, Digestive and Kidney Disease, National Institutes of Health, Building 8, Room 207, Bethesda, Maryland 20892 . Phone: (301), 496-3452 . Fax: (301) 402-0240, http://www.nih.gov/sigs/yeast/wickner.html
SP englisch
PO USA
OR Prion-Krankheiten M