Grumbt, Barbara
Stroobant, Vincent
[UCL]
Terziyska, Nadia
Israel, Lars
Hell, Kai
Mia40p and Erv1p are components of a translocation pathway for the import of cysteine-rich proteins into the intermembrane space of mitochondria. We have characterized the redox behavior of Mia40p and reconstituted the disulfide transfer system of Mia40p by using recombinant functional C-terminal fragment of Mia40p, Mia40C, and Erv1p. Oxidized Mia40p contains three intramolecular disulfide bonds. One disulfide bond connects the first two cysteine residues in the CPC motif. The second and the third bonds belong to the twin CX9C motif and bridge the cysteine residues of two CX9C segments. In contrast to the stabilizing disulfide bonds of the twin CX9C motif, the first disulfide bond was easily accessible to reducing agents. Partially reduced Mia40C generated by opening of this bond as well as fully reduced Mia40C were oxidized by Erv1p in vitro. In the course of this reaction, mixed disulfides of Mia40C and Erv1p were formed. Reoxidation of fully reduced Mia40C required the presence of the first two cysteine residues in Mia40C. However, efficient reoxidation of a Mia40C variant containing only the cysteine residues of the twin CX9C motif was observed when in addition to Erv1p low amounts of wild type Mia40C were present. In the reconstituted system the thiol oxidase Erv1p was sufficient to transfer disulfide bonds to Mia40C, which then could oxidize the variant of Mia40C. In summary, we reconstituted a disulfide relay system consisting of Mia40C and Erv1p.
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Bibliographic reference |
Grumbt, Barbara ; Stroobant, Vincent ; Terziyska, Nadia ; Israel, Lars ; Hell, Kai. Functional characterization of Mia40p, the central component of the disulfide relay system of the mitochondrial intermembrane space. In: Journal of Biological Chemistry, Vol. 282, no. 52, p. 37461-37470 (2007) |
Permanent URL |
http://hdl.handle.net/2078.1/36919 |