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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.

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Acknowledgments

We thank Irina Derkatch for the pID116 plasmid. This work was supported by a grant from the National Institutes of Health (GM56350 to S.W.L).

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  1. Department of Biological Sciences, University of Illinois at Chicago, 900 S. Ashland M/C 567, Chicago, IL , 60607, USA

    Yakov A. Vitrenko, Mariana E. Pavon, Stephen I. Stone & Susan W. Liebman

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  1. Yakov A. Vitrenko
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  2. Mariana E. Pavon
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  3. Stephen I. Stone
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  4. Susan W. Liebman
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Correspondence to Susan W. Liebman.

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Communicated by M. Kupiec.

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Vitrenko, Y.A., Pavon, M.E., Stone, S.I. et al. Propagation of the [PIN +] prion by fragments of Rnq1 fused to GFP. Curr Genet 51, 309–319 (2007). https://doi.org/10.1007/s00294-007-0127-0

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  • DOI: https://doi.org/10.1007/s00294-007-0127-0

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