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Literature summary for 7.4.2.3 extracted from

  • Boemer, U.; Maarse, A.C.; Martin, F.; Geissler, A.; Merlin, A.; Schoenfisch, B.; Meijer, M.; Pfanner, N.; Rassow, J.
    Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins (1998), EMBO J., 17, 4226-4237.
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion inner mitochondrial membrane Saccharomyces cerevisiae 5739
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Saccharomyces cerevisiae preprotein transport across the mitochondrial inner membrane ADP + phosphate
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Organism

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O 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 Saccharomyces cerevisiae ADP + phosphate
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ATP + H2O preprotein transport across the mitochondrial inner membrane Saccharomyces cerevisiae ADP + phosphate
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Subunits

Subunits Comment Organism
More subunit TIM44 forms a complex with the matrix-heat-shock protein Hsp70 Saccharomyces cerevisiae