Mechanism of prion loss after Hsp104 inactivation in yeast.
about
Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentationYeast prions: protein aggregation is not enoughRole of Heat-Shock Proteins in Cellular Function and in the Biology of FungiActin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in YeastDisaggregases, molecular chaperones that resolubilize protein aggregatesDifferences in the curing of [PSI+] prion by various methods of Hsp104 inactivationHsp104-dependent remodeling of prion complexes mediates protein-only inheritanceMolecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates.The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae.The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotypeCooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.De novo [PSI +] prion formation involves multiple pathways to form infectious oligomers.Modulation of Abeta42 low-n oligomerization using a novel yeast reporter systemHsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.Heterologous prion interactions are altered by mutations in the prion protein Rnq1p.Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prionPrion dynamics and the quest for the genetic determinant in protein-only inheritanceHsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seedsRole for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication.Prion formation and polyglutamine aggregation are controlled by two classes of genes.Curing of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division.Primary sequence independence for prion formation[PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain.Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.Low activity of select Hsp104 mutants is sufficient to propagate unstable prion variantsYeast prion protein derivative defective in aggregate shearing and production of new 'seeds'Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotoleranceYeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104.Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availabilityHsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopyA heritable structural alteration of the yeast mitochondrionDestabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants.Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing.N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpressionMolecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways.Destabilization and recovery of a yeast prion after mild heat shock.
P2860
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P2860
Mechanism of prion loss after Hsp104 inactivation in yeast.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Mechanism of prion loss after Hsp104 inactivation in yeast.
@en
Mechanism of prion loss after Hsp104 inactivation in yeast.
@nl
type
label
Mechanism of prion loss after Hsp104 inactivation in yeast.
@en
Mechanism of prion loss after Hsp104 inactivation in yeast.
@nl
prefLabel
Mechanism of prion loss after Hsp104 inactivation in yeast.
@en
Mechanism of prion loss after Hsp104 inactivation in yeast.
@nl
P2093
P2860
P1476
Mechanism of prion loss after Hsp104 inactivation in yeast.
@en
P2093
P2860
P304
P356
10.1128/MCB.21.14.4656-4669.2001
P407
P577
2001-07-01T00:00:00Z