Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 7.4.2.3 extracted from

  • Schiller, D.; Cheng, Y.C.; Liu, Q.; Walter, W.; Craig, E.A.
    Residues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tethering (2008), Mol. Cell. Biol., 28, 4424-4433.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane
-
Saccharomyces cerevisiae 5743
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae 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 ?
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Saccharomyces cerevisiae ?
-
?

Synonyms

Synonyms Comment Organism
mitochondrial hsp70
-
Saccharomyces cerevisiae