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 | 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrial inner membrane | associated to on the matrix side | Saccharomyces cerevisiae | 5743 | - |
mitochondrial matrix | mainly | Saccharomyces cerevisiae | 5759 | - |
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 | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Saccharomyces cerevisiae | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Saccharomyces cerevisiae | ADP + phosphate | - |
? | |
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 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
mitochondrial hsp70 | - |
Saccharomyces cerevisiae |
mtHSP70 | - |
Saccharomyces cerevisiae |
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 |