Targeting and Maturation of Erv1/ALR in the Mitochondrial Intermembrane Space

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• 作者：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
• 刊名：ACS Chemical Biology
• 出版年：2012
• 出版时间：April 20, 2012
• 年：2012
• 卷：7
• 期：4
• 页码：707-714
• 全文大小：419K
• 年卷期：v.7,no.4(April 20, 2012)
• ISSN：1554-8937

文摘

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.