Propagation of the [PIN + ] prion by fragments of Rnq1 fused to GFP

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Abstract
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.