Propagation of the [PIN+] prion by fragments of Rnq1 fused to GFP.
Prions are viewed as enigmatic infectious entities whose genetic properties are enciphered solely in an array of self-propagating protein aggregate conformations. Rnq1, a yeast protein with yet unknown function, forms a prion named [PIN+] for its ability to facilitate the de novo induction of another prion, [PSI+]. Here we investigate a set of RNQ1 truncations that were designed to cover major Rnq1 sequence elements similar to those important for the propagation of other yeast prions: a region rich in asparagines and glutamines and several types of oligopeptide repeats. Proteins encoded by these RNQ1 truncations were tested for their ability to (a) join (decorate) pre-existing [PIN+] aggregates made of wild-type Rnq1 and (b) maintain the heritable aggregated state in the absence of wild-type RNQ1. While the possible involvement of particular sequence elements in the propagation of [PIN+] is discussed, the major result is that the efficiency of transmission of [PIN+] from wild-type Rnq1 to a fragment decreased with the fragment's length.
Vitrenko
Yakov A
YA
Department of Biological Sciences, University of Illinois at Chicago, 900 S. Ashland M/C 567, Chicago, IL 60607, USA.
Pavon
Mariana E
ME
Stone
Stephen I
SI
Liebman
Susan W
SW
D000483:Alleles; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D049452:Green Fluorescent Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D011328:Prions / Q000737:chemistry / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics*
D011328:Prions; C404807:RNQ1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D049452:Green Fluorescent Proteins