Article

ATP modulates self-perpetuating conformational conversion generating structurally distinct yeast prion amyloids that limit autocatalytic amplification

2022-10-19

Abstract excerpt

Prion-like self-perpetuating conformational conversion of proteins into amyloid aggregates is associated with both transmissible neurodegenerative diseases and non-Mendelian inheritance. Here, we demonstrate that ATP modulates the formation and dissolution of amyloids from a yeast prion domain (NM domain of Saccharomyces cerevisiae Sup35) and restricts autocatalytic amplification by controlling the amount of frag...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 0896f174-a984-5f5c-850f-ac11eff6bae4
DOI: 10.1101/2022.10.19.512876

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

ATP modulates self-perpetuating conformational conversion generating structurally distinct yeast prion amyloids that limit autocatalytic amplificationDOI 10.1101/2022.10.19.512876Read

Sub-stoichiometric Hsp104 regulates the genesis and persistence of self-replicable amyloid seeds of a yeast prion proteinSemantic proximity Read

The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation.Semantic proximity Read

Conserved features of intermediates in amyloid assembly determine their benign or toxic statesSemantic proximity Read

Distinct amino acid compositional requirements for formation and maintenance of the [PSI⁺] prion in yeast.Semantic proximity Read

Threshold inclusion size triggers conversion of huntingtin to prion-like state that is reversible in newly born cellsSemantic proximity Read

Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities.Semantic proximity Read

Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation.Semantic proximity Read

Prion Replication in the Mammalian Cytosol: Functional Regions within a Prion Domain Driving Induction, Propagation, and Inheritance.Semantic proximity Read

Soluble oligomers are sufficient for transmission of a yeast prion but do not confer phenotype.Semantic proximity Read

The physical dimensions of amyloid aggregates control their infective potential as prion particles.Semantic proximity Read

Prion-like disorders: blurring the divide between transmissibility and infectivitySemantic proximity Read

ATP enhances at low concentrations but dissolves at high concentrations liquid-liquid phase separation (LLPS) of ALS/FTD-causing FUS.Semantic proximity Read