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ATP + H2O
ADP + phosphate
ATP + H2O + dihydrofolate reductase[side 1]
ADP + phosphate + dihydrofolate reductase[side 2]
-
-
-
-
?
ATP + H2O + heat shock protein 70[side 1]
ADP + phosphate + heat shock protein 70[side 2]
-
-
-
-
?
ATP + H2O + heat shock protein 90[side 1]
ADP + phosphate + heat shock protein 90[side 2]
-
-
-
-
?
ATP + H2O + mitochondrial preprotein pFAD[side 1]
ADP + phosphate + mitochondrial preprotein pFAD[side 2]
-
-
-
-
?
ATP + H2O + mitochondrial-protein[side 1]
ADP + phosphate + mitochondrial-protein[side 2]
-
-
-
-
?
ATP + H2O + protein/out
ADP + phosphate + protein/in
additional information
?
-
ATP + H2O
ADP + phosphate
-
ATP hydrolysis needed by Bcl-2 associated athanogene 1M (Bag-1M), which interacts with the ATPase domain of Hsp70 to modulate the release of the substrate from Hsp70. ATP hydrolysis enhances Bag-1M-mediated inhibition of the DNA binding by the glucocorticoid receptor GR
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
several rounds of ATP-dependent binding to and release from mtHsp70 lead to complete translocation of polypeptides into the mitochondrial matrix
-
-
?
ATP + H2O
ADP + phosphate
-
Hsp70 escort proteins are essential for maintaining the function of yeast mitochondrial hsp70 molecular chaperones(mtHsp70)
-
-
?
ATP + H2O
ADP + phosphate
-
mtHsp70 exhibits limited solubility due to aggregation mediated by its ATPase domain, residues 47-440, but human escort protein Hep directly enhances chaperone solubility through interactions with this domain
-
-
?
ATP + H2O
ADP + phosphate
-
human mtHsp70 exhibits limited solubility due to aggregation mediated by its ATPase domain and show that human Hep directly enhances chaperone solubility through interactions with this domain
-
-
?
ATP + H2O
ADP + phosphate
-
the human escort protein Hep binds to the ATPase domain, residues 47-440, of mitochondrial Hsp70 and regulates ATP hydrolysis
-
-
?
ATP + H2O
ADP + phosphate
-
binding of the client proteins to the SBD, substrate binding domain of the mtHsp70 brings a global change in the ATPase domain, thus enhancing the rate of ATP hydrolysis of Hsp70
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
the concerted action of Tim44 and matrix-heat-shock protein Hsp70 drives unfolding of preproteins and accelerates translocation of loosely folded preproteins. While mtHsp70 is essential for import of both tightly and loosely folded preproteins, Tim44 plays a more specialized role in translocation of tightly folded domains
-
?
ATP + H2O
ADP + phosphate
-
preprotein transport across the mitochondrial inner membrane
-
?
ATP + H2O
ADP + phosphate
-
preprotein transport across the mitochondrial inner membrane
-
?
ATP + H2O
ADP + phosphate
-
preprotein transport across the mitochondrial inner membrane
-
?
ATP + H2O
ADP + phosphate
-
preprotein transport across the mitochondrial inner membrane
-
?
ATP + H2O
ADP + phosphate
-
preprotein transport across the mitochondrial inner membrane
-
?
ATP + H2O
ADP + phosphate
-
preprotein transport across the mitochondrial inner membrane
-
?
ATP + H2O
ADP + phosphate
-
activity of mtHsp70 higher than that of DnaK
-
-
?
ATP + H2O
ADP + phosphate
-
ATP appears more favourable for mtHsp70 binding to GST-Tim15 than ADP, ruling out that GST-Tim15 is non-specifically trapped by mtHsp70 as an unfolded chaperone substrate
-
-
?
ATP + H2O
ADP + phosphate
-
the essential mitochondrial Hsp70 is required for the import of mitochondrial preproteins into the matrix compartment. The translocation, specific activity of mitochondrial Hsp70 is coordinated by its interaction with specific partner proteins, forming the import motor complex that provides the energy for unfolding and complete translocation of precursor polypeptide chains. Impaired interdomain communication in mitochondrial Hsp70 results in the loss of inward-directed translocation force
-
-
?
ATP + H2O
ADP + phosphate
-
Hsp70-type chaperones show nucleotide-regulated affinity to polypeptide substrates, allosteric regulation in the course of preprotein translocation. Import of radio-labeled preprotein b2-DHFR fusion protein
-
-
?
ATP + H2O
ADP + phosphate
-
preprotein import-driving ATPase activity of mtHsp70
-
-
?
ATP + H2O
ADP + phosphate
-
ATP appears more favourable for mtHsp70 binding to GST-Tim15 than ADP, ruling out that GST-Tim15 is non-specifically trapped by mtHsp70 as an unfolded chaperone substrate
-
-
?
ATP + H2O + protein/out
ADP + phosphate + protein/in
-
mitochondrial preproteins synthesized in the cytosol are imported through the mitochondrial outer membrane by the translocase of the outer mitochondrial membrane, TOM, complex
-
-
ir
ATP + H2O + protein/out
ADP + phosphate + protein/in
-
-
-
-
ir
ATP + H2O + protein/out
ADP + phosphate + protein/in
-
Tim14 and Tim16 are essential components of the import motor of the mitochondrial TIM23 preprotein translocase, the J and J-like domains of Tim14 and 16 function in the regulation of the ATPase activity of the Hsp70 chaperone of the import motor, with the help of Tim44, Tim14, Tim16 and Mge1 mtHsp70 converts the energy of ATP hydrolysis into vectorial movement of the unfolded polypeptide chain across the translocation pore
-
-
ir
additional information
?
-
-
escort proteins regulate the catalytic activity and solubility of their cognate chaperones, and both forms of regulation arise from interactions with the mtHsp70 ATPase domain, residues 47-440
-
-
?
additional information
?
-
-
newly synthesized mitochondrial precursor proteins have to become unfolded by the mitochondrial Hsp70 import motor to cross the mitochondrial membranes, unfolding mechanism, overview
-
-
?
additional information
?
-
-
an essential peripheral membrane protein, Tim44, tethers mtHsp70, the core of the import motor, to the translocon. The presequence translocase-associated motor complex, PAM, acts as a functional unit to couple the action of mitochondrial Hsp70 chaperone Ssc1 to the movement of preproteins through the Tim23 translocon into the mitochondrial matrix. Tim44-mtHsp70 interaction is destabilized by binding of mtHsp70 to a substrate polypeptide. The N-terminal 167-amino-acid segment of mature Tim44 is suf?cient for both interaction with mtHsp70 and destabilization of a Tim44-mtHsp70 complex caused by client protein binding, mutational interaction analysis, overview
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?
additional information
?
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-
even a partial disruption of the interdomain communication in the mtHsp70 chaperone results in an almost complete breakdown of its translocation-driving properties
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?
additional information
?
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-
interaction of mtHsp70 with partner proteins Mdj1, Mge1, and Tim44
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?
additional information
?
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-
the active presequence translocase drives motor-dependent mitochondrial protein translocation
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?
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Translocation of proteins across the mitochondrial inner membrane, but not into the outer membrane, required nucleoside triphosphates in the matrix
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Saccharomyces cerevisiae
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279
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11
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Saccharomyces cerevisiae
brenda
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J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix
Proc. Natl. Acad. Sci. USA
100
13839-13844
2003
Saccharomyces cerevisiae
brenda
Wadhwa, R.; Takano, S.; Kaur, K.; Aida, S.; Yaguchi, T.; Kaul, Z.; Hirano, T.; Taira, K.; Kaul, S.C.
Identification and characterization of molecular interactions between mortalin/mtHsp70 and HSP60
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391
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Homo sapiens
brenda
Moro, F.; Fernandez-Saiz, V.; Slutsky, O.; Azem, A.; Muga, A.
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272
3184-3196
2005
Saccharomyces cerevisiae
brenda
Mokranjac, D.; Neupert, W.
Protein import into mitochondria
Biochem. Soc. Trans.
33
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2005
Homo sapiens
brenda
Chacinska, A.; Lind, M.; Frazier, A.E.; Dudek, J.; Meisinger, C.; Geissler, A.; Sickmann, A.; Meyer, H.E.; Truscott, K.N.; Guiard, B.; Pfanner, N.; Rehling, P.
Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17
Cell
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817-829
2005
Saccharomyces cerevisiae
brenda
Papatheodorou, P.; Doma?ska, G.; Oxle, M.; Mathieu, J.; Selchow, O.; Kenny, B.; Rassow, J.
The enteropathogenic Escherichia coli (EPEC) Map effector is imported into the mitochondrial matrix by the TOM/Hsp70 system and alters organelle morphology
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8
677-689
2006
Saccharomyces cerevisiae
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25
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Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH499
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Saccharomyces cerevisiae, Saccharomyces cerevisiae PK81
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Mus musculus
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Protein import, replication, and inheritance of a vestigial mitochondrion
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Giardia intestinalis, Giardia intestinalis WB / CC 30957
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Saccharomyces cerevisiae
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Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4743
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44
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