期刊
MICROBIAL CELL
卷 1, 期 3, 页码 81-93出版社
SHARED SCIENCE PUBLISHERS OG
DOI: 10.15698/mic2014.01.130
关键词
cysteine oxidation; disulfide bonds; Dre2; Fe-S clusters; Mia40; mitochondria; oxidative protein folding
资金
- NIH [R37DK053953]
- Deutsche Forschungsgemeinschaft [He2803/4-2, IRTG1830]
- Landesschwerpunkt fur Membrantransport Rheinland-Pfalz
In most cellular compartments cysteine residues are predominantly reduced. However, in the bacterial periplasm, the ER and the mitochondrial intermembrane space (IMS), sulfhydryl oxidases catalyze the formation of disulfide bonds. Nevertheless, many IMS proteins contain reduced cysteines that participate in binding metal-or heme-cofactors. In this study, we addressed the substrate specificity of the mitochondrial protein oxidation machinery. Dre2 is a cysteine-rich protein that is located in the cytosol. A large fraction of Dre2 bound to the cytosolic side of the outer membrane of mitochondria. Even when Dre2 is artificially targeted to the IMS, its cysteine residues remain in the reduced state. This indicates that protein oxidation in the IMS of mitochondria is not a consequence of the apparent oxidizing environment in this compartment but rather is substrate-specific and determined by the presence of Mia40-binding sites.
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