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Literature summary for 4.2.1.3 extracted from

  • Ben-Menachem, R.; Wang, K.; Marcu, O.; Yu, Z.; Lim, T.K.; Lin, Q.; Schueler-Furman, O.; Pines, O.
    Yeast aconitase mitochondrial import is modulated by interactions of its C and N terminal domains and Ssa1/2 (Hsp70) (2018), Sci. Rep., 8, 5903 .
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol localized both to the cytosol and mitochondria by a reverse translocation mechanism Saccharomyces cerevisiae 5829
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mitochondrion localized both to the cytosol and mitochondria by a reverse translocation mechanism Saccharomyces cerevisiae 5739
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P19414
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General Information

General Information Comment Organism
physiological function the aconitase N and C-terminal domains interact and this interaction is important for efficient aconitase posttranslational import into mitochondria and for aconitase dual targeting to mitochondria and cytosol. The C-terminal domain may have a chaperone-like function towards the N-terminal domains, which can be modulated by cytosolic Hsp70 protein Ssa1/2 Saccharomyces cerevisiae