ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2013
Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2.
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2013. 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.
- Effect of evolution of the C-terminal region on chaperone activity of Hsp70.Protein science : a publication of the Protein Society · 2023Article
- Aβ receptors specifically recognize molecular features displayed by fibril ends and neurotoxic oligomers.Nature communications · 2021Article
- Single Molecule Characterization of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2021Review
- The C-terminal GGAP motif of Hsp70 mediates substrate recognition and stress response in yeast.The Journal of biological chemistry · 2018Article
- Cooperative Assembly of Hsp70 Subdomain Clusters.Biochemistry · 2018Article
- Hsp70 Inhibits the Nucleation and Elongation of Tau and Sequesters Tau Aggregates with High Affinity.ACS chemical biology · 2018Article
- Direct Observation of Oligomerization by Single Molecule Fluorescence Reveals a Multistep Aggregation Mechanism for the Yeast Prion Protein Ure2.Journal of the American Chemical Society · 2018Article
- Peptides as Potential Therapeutics for Alzheimer's Disease.Molecules (Basel, Switzerland) · 2018Review
- Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation.The Journal of biological chemistry · 2017Article
- Amphiphilic copolymers reduce aggregation of unfolded lysozyme more effectively than polyethylene glycol.Physical biology · 2017Article
- Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity.Frontiers in molecular neuroscience · 2017Review
- Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation.Nature communications · 2016Article
- Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform.Biophysical journal · 2016Article
- Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.Chemical communications (Cambridge, England) · 2015Review
- Protein Folding and Mechanisms of Proteostasis.International journal of molecular sciences · 2015Review
- Enzymatically Active Microgels from Self-Assembling Protein Nanofibrils for Microflow Chemistry.ACS nano · 2015Article
- Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments.Molecular biology of the cell · 2015Article
- Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The amyloid state and its association with protein misfolding diseases.Nature reviews. Molecular cell biology · 2014Review
- Chaperones: needed for both the good times and the bad times.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
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14 authors.
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Abstract
Ure2p is the protein determinant of the Saccharomyces cerevisiae prion state [URE3]. Constitutive overexpression of the HSP70 family member SSA1 cures cells of [URE3]. Here, we show that Ssa1p increases the lag time of Ure2p fibril formation in vitro in the presence or absence of nucleotide. The presence of the HSP40 co-chaperone Ydj1p has an additive effect on the inhibition of Ure2p fibril formation, whereas the Ydj1p H34Q mutant shows reduced inhibition alone and in combination with Ssa1p. In order to investigate the structural basis of these effects, we constructed and tested an Ssa1p mutant lacking the ATPase domain, as well as a series of C-terminal truncation mutants. The results indicate that Ssa1p can bind to Ure2p and delay fibril formation even in the absence of the ATPase domain, but interaction of Ure2p with the substrate-binding domain is strongly influenced by the C-terminal lid region. Dynamic light scattering, quartz crystal microbalance assays, pull-down assays and kinetic analysis indicate that Ssa1p interacts with both native Ure2p and fibril seeds, and reduces the rate of Ure2p fibril elongation in a concentration-dependent manner. These results provide new insights into the structural and mechanistic basis for inhibition of Ure2p fibril formation by Ssa1p and Ydj1p.
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