Literature summary for 3.6.4.10 extracted from

Mosser, D.D.; Ho, S.; Glover, J.R.
Saccharomyces cerevisiae Hsp104 enhances the chaperone capacity of human cells and inhibits heat stress-induced proapoptotic signaling (2004), Biochemistry, 43, 8107-8115.

Cloned(Commentary)

Cloned (Comment)	Organism
Hsp104 is expressed as a transgene in a human leukemic T-cell line (PEER). Hsp104 inhibited heat-shock-induced loss of viability in PEER cells, and Hsp104 cooperates with endogenous human Hsp70 and Hsc70 molecular chaperones and their J-domain-containing cochaperones Hdj1 and Hdj2 to produce a functional hybrid bichaperone network capable of refolding aggregated luciferase. Hsp104 shuttles across the nuclear envelope and enhances the chaperoning capacity of both the cytoplasm and nucleoplasm of intact cells	Saccharomyces cerevisiae

Cloned (Comment)

Organism

Hsp104 is expressed as a transgene in a human leukemic T-cell line (PEER). Hsp104 inhibited heat-shock-induced loss of viability in PEER cells, and Hsp104 cooperates with endogenous human Hsp70 and Hsc70 molecular chaperones and their J-domain-containing cochaperones Hdj1 and Hdj2 to produce a functional hybrid bichaperone network capable of refolding aggregated luciferase. Hsp104 shuttles across the nuclear envelope and enhances the chaperoning capacity of both the cytoplasm and nucleoplasm of intact cells

Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Saccharomyces cerevisiae	ADP + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
Hsp104	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)