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

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

doi:10.1021/cb200485b.s001

cb200485b_si_001.pdf (993.98 kB)

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

journal contribution

posted on 2012-04-20, 00:00 authored by 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

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.