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Processing of proteins by the molecular chaperone Hsp104.
TLDR
The results reveal that ATP binding to NBD1 serves as a central regulatory switch for the chaperone; it triggers binding of polypeptides, and stimulates ATP hydrolysis in the C-terminal NBD2 by more than two orders of magnitude, implying that ATP hydroolysis in this domain is important for disaggregation. Expand
The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104*
TLDR
It is strongly suggested that guanidinium chloride causes curing of yeast prions by perturbing the ATPase of Hsp104, which is essential for both prion propagation and thermotolerance. Expand
Disassembling Protein Aggregates in the Yeast Cytosol
TLDR
It is shown that recovery of proteins from aggregates in the cell requires the chaperones to work together with defined but overlapping functions, and the results are consistent with a model of several interrelated defense lines against protein aggregation. Expand
Substrate Binding to the Molecular Chaperone Hsp104 and Its Regulation by Nucleotides*
TLDR
The interaction of Hsp104 with reduced, carboxymethylated α-lactalbumin (RCMLa), a permanently unfolded model substrate, is investigated and it is demonstrated that the affinity of HSp104 toward polypeptides is regulated by nucleotides, and upon association with a polypeptic, a conformational change occurs within Hsp 104 that strongly reduces the dynamics of nucleotide exchange and commits the bound polypePTide to ATP hydrolysis. Expand
Regulatory Circuits of the AAA+ Disaggregase Hsp104
TLDR
A sophisticated allosteric network consisting of three distinct pathways that senses the nucleotide state of AAA+ modules and transmits this information across the Hsp104 hexamer is identified and the first comprehensive map of nucleotide-related allosterics signals in a class-1 AAA+ protein is provided. Expand
The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle.
TLDR
A model is proposed that correlates the ordered assembly of the Hsp90 co-chaperones with distinct steps of the ATP hydrolysis reaction during the chaperone cycle. Expand
Characteristics of an exochitinase from Streptomyces olivaceoviridis, its corresponding gene, putative protein domains and relationship to other chitinases.
TLDR
The chitin-inducible enzyme with an isoelectric point of 4.0 shows optimal activity at pH 7.3 and 55 degrees C, has an apparent molecular mass of 47 kDa and is competitively inhibited by the pseudosugar allosamidin. Expand
The molecular chaperone Hsp104--a molecular machine for protein disaggregation.
TLDR
Hsp104 is an ATP dependent molecular machine that-in cooperation with Hsp70 and Hsp40-extracts polypeptide chains from protein aggregates and facilitates their refolding, although the molecular details of this process are still poorly understood. Expand
The gene encoding the cellulase (Avicelase) Cell from Streptomyces reticuli and analysis of protein domains
TLDR
Comparison of the W‐terminal amino acids from the purified proteins with the amino acid sequence derived from the Avicelase gene revealed that the truncated enzyme corresponds to the C‐ terminal region whereas the inactive proteolytically derived protein represents the N‐terminus of the 82 kDa AvicELase. Expand
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