Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions
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Yeast prions: structure, biology, and prion-handling systemsYeast prions are useful for studying protein chaperones and protein quality controlCooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregationHeat shock protein 104 (Hsp104)-mediated curing of [PSI+] yeast prions depends on both [PSI+] conformation and the properties of the Hsp104 homologs.Prion propagation can occur in a prokaryote and requires the ClpB chaperone.Sporadic distribution of prion-forming ability of Sup35p from yeasts and fungi.Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation.Functional diversification of hsp40: distinct j-protein functional requirements for two prions allow for chaperone-dependent prion selectionHsp40 function in yeast prion propagation: Amyloid diversity necessitates chaperone functional complexity.Structural variants of yeast prions show conformer-specific requirements for chaperone activity.Human J-protein DnaJB6b Cures a Subset of Saccharomyces cerevisiae Prions and Selectively Blocks Assembly of Structurally Related Amyloids.Schizosaccharomyces pombe disaggregation machinery chaperones support Saccharomyces cerevisiae growth and prion propagation.Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor.Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation.Transcription regulation of HYPK by Heat Shock Factor 1Physiological and environmental control of yeast prions.ClpB/Hsp100 proteins and heat stress tolerance in plants.Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions.Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients.Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation.Hsp104 disaggregase at normal levels cures many [PSI+] prion variants in a process promoted by Sti1p, Hsp90, and Sis1p.Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria.To CURe or not to CURe? Differential effects of the chaperone sorting factor Cur1 on yeast prions are mediated by the chaperone Sis1.Chaperone functional specificity promotes yeast prion diversity.
P2860
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P2860
Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Prokaryotic chaperones support ...... egation machinery interactions
@ast
Prokaryotic chaperones support ...... egation machinery interactions
@en
type
label
Prokaryotic chaperones support ...... egation machinery interactions
@ast
Prokaryotic chaperones support ...... egation machinery interactions
@en
prefLabel
Prokaryotic chaperones support ...... egation machinery interactions
@ast
Prokaryotic chaperones support ...... egation machinery interactions
@en
P2860
P921
P1433
P1476
Prokaryotic chaperones support ...... egation machinery interactions
@en
P2093
Daniel C Masison
P2860
P304
P356
10.1534/GENETICS.112.142307
P407
P577
2012-06-25T00:00:00Z