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Literature summary for 7.4.2.3 extracted from
- Conformational properties of bacterial DnaK and yeast mitochondrial Hsp70. Role of the divergent C-terminal alpha-helical subdomain (2005), FEBS J., 272, 3184-3196.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| DnaJ | bacterial co-chaperone stimulates ATPase activity of mtHsp70 5fold, that of DnaK 20fold | Saccharomyces cerevisiae | |
| fluorescein-CALLQSRLLLSAPRRAAATARY | similar affininty of mtHsp70 and Dnak at 25°C | Saccharomyces cerevisiae |  |
| GrpE | bacterial co-chaperone stimulates ATPase activity of mtHsp70 5fold, that of DnaK 20fold | Saccharomyces cerevisiae | |
| KCCC | comparable stimulation of ATPase activity of mtHsp70 and Dnak | Saccharomyces cerevisiae | |
| KKCC | comparable stimulation of ATPase activity of mtHsp70 and Dnak | Saccharomyces cerevisiae | |
| Mdj1p | mitochondrial co-chaperone stimulates ATPase activity of both mtHsp70 and Dnak 5-6fold, 20fold activation can be achieved by different molar ratios | Saccharomyces cerevisiae | |
| Mge1p | mitochondrial co-chaperone stimulates ATPase activity of both mtHsp70 and Dnak 5-6fold, 20fold activation can be achieved by different molar ratios | Saccharomyces cerevisiae | |
| NRLLLTG | substrate binding allosterically stimulates ATPase activity of mtHsp70 2.5 fold, that of Dnak 5fold | Saccharomyces cerevisiae | |
Application
| Application | Comment | Organism |
|---|---|---|
| additional information | mtHsp70 and Escherichia coli DnaK display different conformational and biochemical properties, chimeric Hsp70s can not complement DnaK function in vivo | Saccharomyces cerevisiae |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| chimeric Hsp70s overexpressed in BB1553 cells, mtHsp70 overexpressed in the yeast strain YKN3B | Saccharomyces cerevisiae |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| inner membrane | - |
Saccharomyces cerevisiae | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 44000 | - |
SDS-PAGE, possibly the ATPase domain of mtHsp70 | Saccharomyces cerevisiae |
| 58000 | - |
SDS-PAGE, fragment in the presence of ATP | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| by ion exchange, ATP-agarose affinity and hydroxyapatite chromatographies | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | activity of mtHsp70 higher than that of DnaK | Saccharomyces cerevisiae | ADP + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| mitochondrial hsp70 | - |
Saccharomyces cerevisiae |
| mtHSP70 | - |
Saccharomyces cerevisiae |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 76.2 | mtHsp70 binding kinetics are faster at higher temperatures | Saccharomyces cerevisiae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 51.6 | - |
thermal denaturation of mtHsp70 shows three endotherms centered at 51.6, 67.5 and 76.2°C, the endotherm at 51.6°C may represent the unfolding of a more stable ATPase domain | Saccharomyces cerevisiae |
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