ArticlePLoS genetics2010
Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1.
Article in PLoS genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Transcriptomic analysis of Rnq1 loss and prionization reveals alterations in translation pathways and energy metabolism.Scientific reports · 2026Article
- Mapping of Prion Structures in the Yeast Rnq1.International journal of molecular sciences · 2024Article
- Article
- Overproduction of Sch9 leads to its aggregation and cell elongation in Saccharomyces cerevisiae.PloS one · 2018Article
- Predicting Amyloidogenic Proteins in the Proteomes of Plants.International journal of molecular sciences · 2017Article
- Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae.Scientific reports · 2017Article
- Article
- Prions, amyloids, and RNA: Pieces of a puzzle.Prion · 2016Review
- Effect of domestication on the spread of the [PIN+] prion in Saccharomyces cerevisiae.Genetics · 2014Article
- Yeast prions and human prion-like proteins: sequence features and prediction methods.Cellular and molecular life sciences : CMLS · 2014Review
- Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions.PLoS genetics · 2014Article
- An insight into the complex prion-prion interaction network in the budding yeast Saccharomyces cerevisiae.Prion · 2014Article
- Exploring the basis of [PIN(+)] variant differences in [PSI(+)] induction.Journal of molecular biology · 2013Article
- Sex, prions, and plasmids in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Prions in yeast.Genetics · 2012Review
- Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity.Molecular and cellular biology · 2012Article
- A small, glutamine-free domain propagates the [SWI(+)] prion in budding yeast.Molecular and cellular biology · 2011Article
- The prion hypothesis: from biological anomaly to basic regulatory mechanism.Nature reviews. Molecular cell biology · 2010Review
- Distinct subregions of Swi1 manifest striking differences in prion transmission and SWI/SNF function.Molecular and cellular biology · 2010Article
- Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission.Molecular microbiology · 2010Article
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3 authors.
Funding
Abstract
Prions are self-propagating protein conformations. Transmission of the prion state between non-identical proteins, e.g. between homologous proteins from different species, is frequently inefficient. Transmission barriers are attributed to sequence differences in prion proteins, but their underlying mechanisms are not clear. Here we use a yeast Rnq1/[PIN(+)]-based experimental system to explore the nature of transmission barriers. [PIN(+)], the prion form of Rnq1, is common in wild and laboratory yeast strains, where it facilitates the appearance of other prions. Rnq1's prion domain carries four discrete QN-rich regions. We start by showing that Rnq1 encompasses multiple prion determinants that can independently drive amyloid formation in vitro and transmit the [PIN(+)] prion state in vivo. Subsequent analysis of [PIN(+)] transmission between Rnq1 fragments with different sets of prion determinants established that (i) one common QN-rich region is required and usually sufficient for the transmission; (ii) despite identical sequences of the common QNs, such transmissions are impeded by barriers of different strength. Existence of transmission barriers in the absence of amino acid mismatches in transmitting regions indicates that in complex prion domains multiple prion determinants act cooperatively to attain the final prion conformation, and reveals transmission barriers determined by this cooperative fold.
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