Hsp104, Hsp70, and Hsp40: A Novel Chaperone System that Rescues Previously Aggregated Proteins
John R Glover,Susan Lindquist +1 more
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TLDR
It is concluded that Hsp104 has a protein remodeling activity that acts on trapped, aggregated proteins and requires specific interactions with conventional chaperones to promote refolding of the intermediates it produces.About:
This article is published in Cell.The article was published on 1998-07-10 and is currently open access. It has received 1360 citations till now. The article focuses on the topics: Co-chaperone & Chaperone (protein).read more
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Hsp70 chaperones: cellular functions and molecular mechanism.
Matthias P. Mayer,Bernd Bukau +1 more
TL;DR: This work has shown that for specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100, and this ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target H Sp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the HSp70-substrate complex.
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Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response
TL;DR: The significance of Hsps and chaperones in abiotic stress responses in plants is summarized, and the co-operation among their different classes and their interactions with other stress-induced components are discussed.
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Protein degradation and protection against misfolded or damaged proteins
TL;DR: A full understanding of the pathogenesis of the protein-folding diseases will require greater knowledge of how misfolded proteins are recognized and selectively degraded.
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AAA+: A Class of Chaperone-Like ATPases Associated with the Assembly, Operation, and Disassembly of Protein Complexes
TL;DR: Whole-genome analysis indicates that this class of proteins is ancient and has undergone considerable functional divergence prior to the emergence of the major divisions of life.
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Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease
TL;DR: Direct expression of the molecular chaperone Hsp70 prevented dopaminergic neuronal loss associated with α-synuclein in Drosophila and that interference with endogenous chaper one activity accelerated α- synuclein toxicity, suggesting chaperones may play a role in Parkinson's disease progression.
References
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A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae.
Robert S. Sikorski,Philip Hieter +1 more
TL;DR: A series of yeast shuttle vectors and host strains has been created to allow more efficient manipulation of DNA in Saccharomyces cerevisiae to perform most standard DNA manipulations in the same plasmid that is introduced into yeast.
Journal Article
A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae.
Journal ArticleDOI
Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+].
TL;DR: It is reported that an intermediate amount of the chaperone protein Hsp104 was required for the propagation of the yeast non-Mendelian factor [psi+], and that a certain level of chaper one expression can cure cells of prions without affecting viability.
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Protein disaggregation mediated by heat-shock protein Hsp104.
TL;DR: Hspl04 functions in a manner not previously described for other heat-shock proteins: it mediates the resolubilization of heat-inactivated luciferase from insoluble aggregates.
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HSP104 required for induced thermotolerance.
Yolanda Sánchez,Susan Lindquist +1 more
TL;DR: It is demonstrated that a particular heat shock protein plays a critical role in cell survival at extreme temperatures and is rescued with the wild-type gene.