期刊
ACS CHEMICAL BIOLOGY
卷 7, 期 4, 页码 707-714出版社
AMER CHEMICAL SOC
DOI: 10.1021/cb200485b
关键词
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资金
- EC (Bio-NMR) [261863]
- Italian MIUR-FIRB PROTEOMICA-RBRN07BMCT
- IMBB-FORTH
- University of Crete
- European Social Fund
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 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.
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