Targeting and Maturation of Erv1/ALR in the Mitochondrial Intermembrane Space
| Autor: | Lucia Banci, Charalambos Pozidis, Riccardo Peruzzini, Kostas Tokatlidis, Maria Andreadaki, Simone Ciofi-Baffoni, Karolina Gajda, Emmanouela Kallergi, Chiara Cefaro, Nitsa Katrakili, Paraskevi Kritsiligkou, Ivano Bertini |
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| Rok vydání: | 2012 |
| Předmět: |
Protein Folding
Mitochondrial intermembrane space Mitochondrion Mitochondrial Membrane Transport Proteins Biochemistry 03 medical and health sciences Mitochondrial membrane transport protein chemistry.chemical_compound 0302 clinical medicine Mitochondrial Precursor Protein Import Complex Proteins Humans Oxidoreductases Acting on Sulfur Group Donors Disulfides Protein maturation Cytochrome Reductases 030304 developmental biology Flavin adenine dinucleotide 0303 health sciences biology General Medicine Transport protein Cell biology Protein Transport chemistry Mitochondrial Membranes Flavin-Adenine Dinucleotide biology.protein Molecular Medicine Protein folding Intermembrane space 030217 neurology & neurosurgery |
| Zdroj: | ACS Chemical Biology. 7:707-714 |
| ISSN: | 1554-8937 1554-8929 |
| DOI: | 10.1021/cb200485b |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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