Document Type
Article
Publication Date
2012
Abstract
The Mia40 import pathway facilitates the import and oxidative folding of cysteine-rich protein substrates into the mitochondrial intermembrane space. Here we describe the in vitro and in organello oxidative folding of Cmc1, a twin CX9C-containing substrate, which contains an unpaired cysteine. In vitro, Cmc1 can be oxidized by the import receptor Mia40 alone when in excess or at a lower rate by only the sulfhydryl oxidase Erv1. However, physiological and efficient Cmc1 oxidation requires Erv1 and Mia40. Cmc1 forms a stable intermediate with Mia40 and is released from this interaction in the presence of Erv1. The three proteins are shown to form a ternary complex in mitochondria. Our results suggest that this mechanism facilitates efficient formation of multiple disulfides and prevents the formation of non-native disulfide bonds.
Original Publication Citation
Bourens M, Dabir DV, Tienson HL, Sorokina I, Koehler CM, Barrientos A. Role of twin Cys-Xaa9-Cys motif cysteines in mitochondrial import of the cytochrome C oxidase biogenesis factor Cmc1. J Biol Chem. 2012 Sep 7;287(37):31258-69. doi: 10.1074/jbc.M112.383562. Epub 2012 Jul 5. PMID: 22767599; PMCID: PMC3438957.
Digital Commons @ LMU & LLS Citation
Dabir, Deepa V., "Role of twin Cys-Xaa9-Cys motif cysteines in mitochondrial import of the cytochrome c oxidase biogenesis factor Cmc1" (2012). Biology Faculty Works. 109.
https://digitalcommons.lmu.edu/bio_fac/109
