Literature summary for 7.4.2.3 extracted from

Moro, F.; Okamoto, K.; Donzeau, M.; Neupert, W.; Brunner, M.
Mitochondrial protein import: Molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44 (2002), J. Biol. Chem., 277, 6874-6880.

Search for more literature for 7.4.2.3

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of chimera of protein with yeast mtHsp70, alpha-helices A and B of the peptide binding domain of mtHsp70 are required to transmit the nucleotide state of the ATPase domain to the peptide domain in yeast mitochondria	Escherichia coli
additional information	construction of chimera of protein with yeast mtHsp70, alpha-helices A and B of the peptide binding domain of mtHsp70 are required to transmit the nucleotide state of the ATPase domain to the peptide domain. Tim44 is proposed to coordinate the binding of mtHsp70 to the incoming preprotein and the subsequent release of the mtHsp70-preprotein complex from the translocase of the inner membrane	Saccharomyces cerevisiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
additional information	after expression in yeast, enzyme with presequence of ATPase subunit 9 of Neurospora crassa is targeted to the matrix of mitochondria and interacts in ATP-independent manner with Tim44	Escherichia coli	-	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	expressed in Saccharomyces cerevisiae	-
Saccharomyces cerevisiae	-	-	-

Synonyms

Synonyms	Comment	Organism
DnaK	-	Escherichia coli
mtHSP70	-	Saccharomyces cerevisiae
Ssc1	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)