ArticleMolecular and cellular biology2011
A small, glutamine-free domain propagates the [SWI(+)] prion in budding yeast.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 21 citations in OpenAlex.
- On the Significance of the Terminal Location of Prion-Forming Regions of Yeast Proteins.International journal of molecular sciences · 2025Article
- Identifying Endogenous Cellular Proteins Destabilizing the Propagation of Swi1 Prion upon Overproduction.Viruses · 2022Article
- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- Defining Key Residues of the Swi1 Prion Domain in Prion Formation and Maintenance.Molecular and cellular biology · 2021Article
- Elucidating the regulatory mechanism of Swi1 prion in global transcription and stress responses.Scientific reports · 2020Article
- Identifying Anti-prion Chemical Compounds Using a Newly Established Yeast High-Throughput Screening System.Cell chemical biology · 2019Article
- A brief overview of the Swi1 prion-[SWI+].FEMS yeast research · 2018Review
- Discovering Putative Prion-Like Proteins inFrontiers in microbiology · 2018Article
- Analysis of Small Critical Regions of Swi1 Conferring Prion Formation, Maintenance, and Transmission.Molecular and cellular biology · 2017Article
- Amino acid composition predicts prion activity.PLoS computational biology · 2017Article
- Emergence and evolution of yeast prion and prion-like proteins.BMC evolutionary biology · 2016Article
- Article
- Yeast prions and human prion-like proteins: sequence features and prediction methods.Cellular and molecular life sciences : CMLS · 2014Review
- Increasing prion propensity by hydrophobic insertion.PloS one · 2014Article
- An insight into the complex prion-prion interaction network in the budding yeast Saccharomyces cerevisiae.Prion · 2014Article
- Transgenerational epigenetic inheritance: how important is it?Nature reviews. Genetics · 2013Review
- Prions in yeast.Genetics · 2012Review
- The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.Brain research · 2012Review
- Diversity, biogenesis and function of microbial amyloids.Trends in microbiology · 2012Review
- Review
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3 authors at 1 institution in 1 country.
Funding
Abstract
Yeast prions are self-propagating protein conformations that transmit heritable phenotypes in an epigenetic manner. The recently identified yeast prion [SWI(+)] is an alternative conformation of Swi1, a component of the evolutionarily conserved SWI/SNF chromatin-remodeling complex. Formation of the [SWI(+)] prion results in a partial loss-of-function phenotype for Swi1. The amino-terminal region of Swi1 is dispensable for its normal function but is required for [SWI(+)] formation and propagation; however, the precise prion domain (PrD) of Swi1 has not been elucidated. Here, we define the minimal Swi1 PrD as the first 37 amino acids of the protein. This region is extremely asparagine rich but, unexpectedly, contains no glutamine residues. This unusually small prion domain is sufficient for aggregation, propagation, and transmission of the [SWI(+)] prion. Because of its unusual size and composition, the Swi1 prion domain defined here has important implications for describing and identifying novel prions.
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