期刊
JOURNAL OF BIOCHEMISTRY
卷 146, 期 5, 页码 599-608出版社
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvp133
关键词
disulphide bond formation; Erv1; intermembrane space; Mia40; protein import
资金
- Deutsche Forschungsgemeinschaft [DE1431/2-1, HE2803/2-4, SFB594/B13]
Proteins of the intermembrane space (IMS) of mitochondria fulfil crucial functions in cellular processes, such as transport of proteins and metal ions, ATP production and apoptotic cell death. All IMS proteins are synthesized in the cytosol and then transported across the mitochondrial outer membrane. A subset of these proteins contains disulphide bonds. For their import into the IMS, they employ a disulphide relay system, made up of two essential proteins, Mia40/Tim40 and the flavin-dependent sulfhydryl-electron transferase Erv1. The disulphide relay system introduces disulphide bonds in substrate proteins triggering their folding. The oxidative folding traps substrates in the IMS and thereby drives their net import into the IMS. Thus, protein import is coupled to oxidative protein folding, maybe providing a first control of protein quality. Here, we review the current knowledge about the Erv1-Mia40 system and address aspects that require further consideration.
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