Targeting and maturation of Erv1/ALR in the mitochondrial intermembrane space

Emmanouela Kallergi, Maria Andreadaki, Paraskevi Kritsiligkou, Nitsa Katrakili, Charalambos Pozidis, Kostas Tokatlidis, Lucia Banci, Ivano Bertini, Chiara Cefaro, Simone Ciofi-Baffoni, Karolina Gajda, Riccardo Peruzzini

    Research output: Contribution to journalArticlepeer-review

    Abstract

    The interaction of Mia40 with Erv1/ALR is central to the oxidative protein folding in the intermembrane space of mitochondria (IMS) as Erv1/ALR oxidizes reduced Mia40 to restore its functional state. Here we address the role of Mia40 in the import and maturation of Erv1/ALR. The C-terminal FAD-binding domain of Erv1/ALR has an essential role in the import process by creating a transient intermolecular disulfide bond with Mia40. The action of Mia40 is selective for the formation of both intra and intersubunit structural disulfide bonds of Erv1/ALR, but the complete maturation process requires additional binding of FAD. Both of these events must follow a specific sequential order to allow Erv1/ALR to reach the fully functional state, illustrating a new paradigm for protein maturation in the IMS.

    Original languageEnglish
    Pages (from-to)707-14
    Number of pages8
    JournalACS chemical biology
    Volume7
    Issue number4
    DOIs
    Publication statusPublished - 20 Apr 2012

    Keywords

    • Cytochrome Reductases
    • Disulfides
    • Flavin-Adenine Dinucleotide
    • Humans
    • Mitochondrial Membrane Transport Proteins
    • Mitochondrial Membranes
    • Protein Folding
    • Protein Transport

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