The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments - PubMed
- ️Fri Jan 01 1999
The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments
H K Edskes et al. Proc Natl Acad Sci U S A. 1999.
Abstract
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.
Figures
Cellular distribution of Ure2-GFP fusion proteins. Into strains YHE64 (3686[URE3]) and 3686[ure-o] were introduced pVTG12 (CEN LEU2 PURE2 URE2N-GFP) (Top), pVTG13 (CEN LEU2 PURE2 GFP-URE2C) (Middle), and pH327 (CEN LEU2 PURE2 URE2-GFP) (Bottom). [ure-o], transformant of 3686[ure-o]; [URE3], transformant of YHE64 that retained [URE3]; GuHCl, transformant of YHE64 that was initially [URE3] but was cured by growth in the presence of 5 mM guanidine HCl. Phase contrast pictures of only the cells with pH327 (Bottom) are shown. The second row of pictures shows further examples of [URE3] cells with pVTG12.
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