2022
DOI: 10.3390/epigenomes6010004
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Biochemical Principles in Prion-Based Inheritance

Abstract: Prions are proteins that can stably fold into alternative structures that frequently alter their activities. They can self-template their alternate structures and are inherited across cell divisions and generations. While they have been studied for more than four decades, their enigmatic nature has limited their discovery. In the last decade, we have learned just how widespread they are in nature, the many beneficial phenotypes that they confer, while also learning more about their structures and modes of inhe… Show more

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Cited by 6 publications
(9 citation statements)
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“…However, the first discovered and well-characterized prion protein, human PrP, also does not contain typical Q/N-rich regions. Other yeast prion-forming proteins linked to the [ ISP + ], [ MOD + ], [ GAR + ], [ ESI + ] and [ BIG + ] phenotypes are also atypical in this context 73 . These atypical prions are poorly conserved in their linear amino acid sequence, but commonly contain intrinsically disordered regions (IDRs) which serve as PrDs to endow the proteins with prion-like behavior.…”
Section: Discussionmentioning
confidence: 99%
“…However, the first discovered and well-characterized prion protein, human PrP, also does not contain typical Q/N-rich regions. Other yeast prion-forming proteins linked to the [ ISP + ], [ MOD + ], [ GAR + ], [ ESI + ] and [ BIG + ] phenotypes are also atypical in this context 73 . These atypical prions are poorly conserved in their linear amino acid sequence, but commonly contain intrinsically disordered regions (IDRs) which serve as PrDs to endow the proteins with prion-like behavior.…”
Section: Discussionmentioning
confidence: 99%
“…Protein conformers (protein isoforms that adopt different 3D conformations) connect genotype and environment and could possibly provide protein-based memory (24). Amyloid aggregateforming prions harbor low-complexity protein regions, enriched in glutamine/asparagine (Q/N) residues, or short amyloid-prone sequences in their prion domains (PrDs) that can propagate prion conformers (95).…”
Section: Swi/snf Conformers and Prion-like Domainsmentioning
confidence: 99%
“…Recently, Dennis and Garcia reviewed both amyloid-forming and non-amyloid-forming prions. 20 Prions can be sustained for many generations. 21 An individual protein that contributes to the prion aggregate is called a "prion protein," and a distinct protein domain that is responsible for prion aggregation is called a prion domain (PrD).…”
Section: Amyloids and Prionsmentioning
confidence: 99%
“…While some proteins can be prions without being amyloid‐based, like intrinsically disordered RNA‐binding proteins in Saccharomyces cerevisiae , 19 here we focus on amyloid‐based prions. Recently, Dennis and Garcia reviewed both amyloid‐forming and non‐amyloid‐forming prions 20 …”
Section: Introductionmentioning
confidence: 99%