NR ADSI
AU Edskes,H.K.; Gray,V.T.; Wickner,R.B.
TI The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments
QU Proceedings of the National Academy of Sciences of the United States of America 1999 Feb 16; 96(4): 1498-503
PT journal article
AB The [URE3] nonchromosomal genetic element is a prion of Ure2p, a regulator of nitrogen catabolism in Saccharomyces cerevisiae. Ure2p1-65 is the prion domain of Ure2p, sufficient to propagate [URE3] in vivo. We show that full length Ure2p-green fluorescent protein (GFP) or a Ure2p1-65-GFP fusion protein is aggregated in cells carrying [URE3] but is evenly distributed in cells lacking the [URE3] prion. This indicates that [URE3] involves a self-propagating aggregation of Ure2p. Overexpression of Ure2p1-65 induces the de novo appearance of [URE3] by 1,000-fold in a strain initially [ure-o], but cures [URE3] from a strain initially carrying the [URE3] prion. Overexpression of several other fragments of Ure2p or Ure2-GFP fusion proteins also efficiently cures the prion. We suggest that incorporation of fragments or fusion proteins into a putative [URE3] "crystal" of Ure2p poisons its propagation.
MH Fungal Proteins/biosynthesis/*genetics; Genetic Complementation Test; Luminescent Proteins/biosynthesis/genetics; Nitrogen/metabolism; Plasmids; Prions/chemistry/*genetics; Recombinant Fusion Proteins/biosynthesis; Repressor Proteins/biosynthesis/genetics; Saccharomyces cerevisiae/*genetics/*metabolism
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