Abstract
Thiol-disulphide redox regulation has a key role during the biogenesis of mitochondrial intermembrane space (IMS) proteins. Only the Cys-reduced form of precursor proteins can be imported into mitochondria, which is followed by disulphide bond formation in the mitochondrial IMS. In contrast to the wealth of knowledge on the oxidation process inside mitochondria, little is known about how precursors are maintained in an import-competent form in the cytosol. Here we provide the first evidence that the cytosolic thioredoxin system is required to maintain the IMS small Tim proteins in reduced forms and facilitate their mitochondrial import during respiratory growth. © 2012 EUROPEAN MOLECULAR BIOLOGY ORGANIZATION.
| Original language | English |
|---|---|
| Pages (from-to) | 916-922 |
| Number of pages | 6 |
| Journal | EMBO reports |
| Volume | 13 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - Oct 2012 |
Keywords
- folding
- mitochondrial import
- oxidoreductase
- redox regulation
- thioredoxin