NR AXDK
AU Vitrenko,Y.A.; Pavon,M.E.; Stone,S.I.; Liebman,S.W.
TI Propagation of the [PIN+] prion by fragments of Rnq1 fused to GFP
QU Current Genetics 2007 May; 51(5): 309-19
PT journal article; research support, n.i.h., extramural
AB 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.
MH Alleles; Amino Acid Motifs; Amino Acid Sequence; Green Fluorescent Proteins/*genetics; Molecular Sequence Data; Prions/chemistry/*genetics; Saccharomyces cerevisiae/*chemistry; Saccharomyces cerevisiae Proteins/chemistry/*genetics
AD Department of Biological Sciences, University of Illinois at Chicago, 900 S. Ashland M/C 567, Chicago, IL 60607, USA.
SP englisch
PO USA