ArticleMolecular biology of the cell2007
Role of Hsp104 in the propagation and inheritance of the [Het-s] prion.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Protein Aggregation and Disaggregation in Cells and Development.Journal of molecular biology · 2021Review
- The HET-S/s Prion Motif in the Control of Programmed Cell Death.Cold Spring Harbor perspectives in biology · 2016Review
- Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion.Frontiers in molecular neuroscience · 2016Article
- Signal transduction by a fungal NOD-like receptor based on propagation of a prion amyloid fold.PLoS biology · 2015Article
- Could α-synuclein amyloid-like aggregates trigger a prionic neuronal invasion?BioMed research international · 2015Review
- Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.PLoS pathogens · 2014Article
- When amyloids become prions.Prion · 2014Article
- 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
- Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Hsp104 and prion propagation.Protein and peptide letters · 2009Review
- Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.BioEssays : news and reviews in molecular, cellular and developmental biology · 2008Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The chaperones of the ClpB/HSP100 family play a central role in thermotolerance in bacteria, plants, and fungi by ensuring solubilization of heat-induced protein aggregates. In addition in yeast, Hsp104 was found to be required for prion propagation. Herein, we analyze the role of Podospora anserina Hsp104 (PaHsp104) in the formation and propagation of the [Het-s] prion. We show that DeltaPaHsp104 strains propagate [Het-s], making [Het-s] the first native fungal prion to be propagated in the absence of Hsp104. Nevertheless, we found that [Het-s]-propagon numbers, propagation rate, and spontaneous emergence are reduced in a DeltaPaHsp104 background. In addition, inactivation of PaHsp104 leads to severe meiotic instability of [Het-s] and abolishes its meiotic drive activity. Finally, we show that DeltaPaHSP104 strains are less susceptible than wild type to infection by exogenous recombinant HET-s(218-289) prion amyloids. Like [URE3] and [PIN(+)] in yeast but unlike [PSI(+)], [Het-s] is not cured by constitutive PaHsp104 overexpression. The observed effects of PaHsp104 inactivation are consistent with the described role of Hsp104 in prion aggregate shearing in yeast. However, Hsp104-dependency appears less stringent in P. anserina than in yeast; presumably because in Podospora prion propagation occurs in a syncitium.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.