ArticleEukaryotic cell2009
Increased [PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae.
Article in Eukaryotic cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Article
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
- Mammalian amyloidogenic proteins promote prion nucleation in yeast.The Journal of biological chemistry · 2018Article
- Article
- The [PSIScientific reports · 2017Article
- Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae.Scientific reports · 2017Article
- Heterologous aggregates promote de novo prion appearance via more than one mechanism.PLoS genetics · 2015Article
- Exploring the basis of [PIN(+)] variant differences in [PSI(+)] induction.Journal of molecular biology · 2013Article
- Variant-specific prion interactions: Complicating factors.Cellular logistics · 2013Article
- Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability.PLoS genetics · 2013Article
- [PSI(+) ] prion variant establishment in yeast.Molecular microbiology · 2012Article
- Prions in yeast.Genetics · 2012Review
- A promiscuous prion: efficient induction of [URE3] prion formation by heterologous prion domains.Genetics · 2009Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
During propagation, yeast prions show a strict sequence preference that confers the specificity of prion assembly. Although propagations of [PSI(+)] and [RNQ(+)] are independent of each other, the appearance of [PSI(+)] is facilitated by the presence of [RNQ(+)]. To explain the [RNQ(+)] effect on the appearance of [PSI(+)], the cross-seeding model was suggested, in which Rnq1 aggregates act as imperfect templates for Sup35 aggregation. If cross-seeding events take place in the cytoplasm of yeast cells, the collision frequency between Rnq1 aggregates and Sup35 will affect the appearance of [PSI(+)]. In this study, to address whether cross-seeding occurs in vivo, a new [PSI(+)] induction method was developed that exploits a protein fusion between the prion domain of Sup35 (NM) and Rnq1. This fusion protein successfully joins preexisting Rnq1 aggregates, which should result in the localization of NM around the Rnq1 aggregates and hence in an increased collision frequency between NM and Rnq1 aggregates. The appearance of [PSI(+)] could be induced very efficiently, even with a low expression level of the fusion protein. This study supports the occurrence of in vivo cross-seeding between Sup35 and Rnq1 and provides a new tool that can be used to dissect the mechanism of the de novo appearance of prions.
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