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Literature summary for 3.6.4.10 extracted from

  • Blamowska, M.; Neupert, W.; Hell, K.
    Biogenesis of the mitochondrial Hsp70 chaperone (2012), J. Cell Biol., 199, 125-135.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.10

Activating Compound

Activating Compound Comment Organism Structure
Hep1 Hsp70 escort protein, interacts with mtHsp70 and is crucial for maintaining native mtHsp70 in its functional state, Hep1 is required for the folding of the ATPase domain of mtHsp70. Folding of mtHsp70 is impaired in mitochondria lacking Hep1 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information construction of a mutant mtHsp70A4, in which the linker residues of mtHsp70 are likewise replaced by four alanine residues. This variant generates in the folding assay only a 35-kD stable fragment that corresponds in size to the peptide-binding domain, the ATPase domain in the mtHsp70A4 mutant is not able to fold into a protease-resistant form Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane associated to on the matrix side Saccharomyces cerevisiae 5743
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mitochondrial matrix mainly Saccharomyces cerevisiae 5759
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additional information biogenesis of mtHsp70 in mitochondria, analysis. mtHsp70 folds rapidly after its import into mitochondria. Both domains are independent folding units. The ATPase domain folds in the context of mtHsp70 only in presence of the interdomain linker, whereas the peptide-binding domain folds without the interdomain linker, model of the folding of mtHsp70, overview Saccharomyces cerevisiae
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Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Saccharomyces cerevisiae
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 ADP + phosphate
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 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
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 Saccharomyces cerevisiae ADP + phosphate
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 ?
additional information effect of nucleotides on the formation of the cross-linked adduct: addition of ATP or ADP after formation of the mtHsp70-Hep1 complex leads to release and addition of ATPgammaS to partial release of mtHsp70 from Hep1, whereas almost no mtHsp70 dissociates from Hep1 upon addition of AMP-PNP Saccharomyces cerevisiae ?
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 ?

Synonyms

Synonyms Comment Organism
mitochondrial hsp70
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 Saccharomyces cerevisiae
mtHSP70
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 Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution the structural organization and the molecular mechanism of Hsp70 chaperones are well conserved Saccharomyces cerevisiae
additional information the N-terminal ATPase domain is connected via a short hydrophobic interdomain linker to a C-terminal peptide-binding domain. The interdomain linker between the ATPase domain and PBD is required for the communication between both domains and affects the native conformation of the ATPase domain Saccharomyces cerevisiae
physiological function the enzyme promotes the folding of proteins mainly in the mitochondrial matrix. Another fraction of mtHsp70 is associated with the translocation channel of the TIM23 translocase on the matrix side of the inner membrane and functions as a central component of the import motor of the translocase Saccharomyces cerevisiae