Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 7.4.2.3 extracted from

  • Blamowska, M.; Sichting, M.; Mapa, K.; Mokranjac, D.; Neupert, W.; Hell, K.
    ATPase domain and interdomain linker play a key role in aggregation of mitochondrial Hsp70 chaperone Ssc1 (2010), J. Biol. Chem., 285, 4423-4431.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
cloned in Escherichia coli, expression of ATPase and co-expression of the Hep1 in plasmids containing Ssc1 constructs Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Saccharomyces cerevisiae 5739
-

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P0CS90
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + mitochondrial-protein[side 1] = ADP + phosphate + mitochondrial-protein[side 2] the mitochondrial Hsp70 chaperone Ssc1 requires the Hsp70 escort protein Hep1, an L-shaped matrix protein with a zinc finger motif Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More the ATPase and peptide binding domain (PBD) of Hsp70 proteins are connected by a linker segment that mediates communication between the domains. The minimal co-chaperone Hep1 binding entity of Ssc1 consists of the ATPase domain and the interdomain linker. The ATPase domain in combination with the interdomain linker is crucial for aggregation of Ssc1, stimulating the ATPase activity. In the absence of Hep1, the ATPase domain with the interdomain linker aggregated Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
mitochondrial Hsp70 chaperone Ssc1
-
Saccharomyces cerevisiae
Ssc1
-
Saccharomyces cerevisiae