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Mia40 combines thiol oxidase and disulfide isomerase activity to efficiently catalyze oxidative folding in mitochondria.

Abstract：

:Mia40 (a mitochondrial import and assembly protein) catalyzes disulfide bond formation in proteins in the mitochondrial intermembrane space. By using Cox17 (a mitochondrial copper-binding protein) as a natural substrate, we discovered that, in the presence of Mia40, the formation of native disulfides is strongly favored. The catalytic mechanism of Mia40 involves a functional interplay between the chaperone site and the catalytic disulfide. Mia40 forms a specific native disulfide in Cox17 much more rapidly than other disulfides, in particular, non-native ones, which originates from the recently described high affinity for hydrophobic regions near target cysteines and the long lifetime of the mixed disulfide. In addition to its thiol oxidase function, Mia40 is active also as a disulfide reductase and isomerase. We found that species with inadvertently formed incorrect disulfides are rebound by Mia40 and reshuffled, revealing a proofreading mechanism that is steered by the conformational folding of the substrate protein.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Koch JR,Schmid FX

doi

10.1016/j.jmb.2014.10.022

subject

Has Abstract

pub_date

2014-12-12 00:00:00

pages

4087-4098

issue

24

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(14)00573-7

journal_volume

426

pub_type

杂志文章

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