Erv1 of Arabidopsis thaliana can directly oxidize mitochondrial intermembrane space proteins in the absence of redox-active Mia40

BMC Biology

Research Article

Johannes M. Herrmann¹  Sandra Backes¹  Valentina Peleh¹  Flavien Zannini²  Nicolas Rouhier² 

[1] Cell Biology, University of Kaiserslautern, Erwin-Schrödinger-Strasse 13, 67663, Kaiserslautern, Germany;Unité Mixte de Recherches 1136 Interactions Arbres-Microorganismes, Université de Lorraine/INRA, Faculté des sciences et technologies, 54500 Vandoeuvre-lès-Nancy, Nancy, France;

关键词: Disulfide bond formation;    Eukaryotic evolution;    Intermembrane space;    Mitochondria;    Oxidative protein folding;    Protein translocation;   

DOI  :  10.1186/s12915-017-0445-8

 received in 2017-08-01, accepted in 2017-10-19,  发布年份 2017

来源: Springer

【 摘 要 】

BackgroundMany proteins of the mitochondrial intermembrane space (IMS) contain structural disulfide bonds formed by the mitochondrial disulfide relay. In fungi and animals, the sulfhydryl oxidase Erv1 ‘generates’ disulfide bonds that are passed on to the oxidoreductase Mia40, which oxidizes substrate proteins. A different structural organization of plant Erv1 proteins compared to that of animal and fungal orthologs was proposed to explain its inability to complement the corresponding yeast mutant.ResultsHerein, we have revisited the biochemical and functional properties of Arabidopsis thaliana Erv1 by both in vitro reconstituted activity assays and complementation of erv1 and mia40 yeast mutants. These mutants were viable, however, they showed severe defects in the biogenesis of IMS proteins. The plant Erv1 was unable to oxidize yeast Mia40 and rather even blocked its activity. Nevertheless, it was able to mediate the import and folding of mitochondrial proteins.ConclusionsWe observed that plant Erv1, unlike its homologs in fungi and animals, can promote protein import and oxidative protein folding in the IMS independently of the oxidoreductase Mia40. In accordance to the absence of Mia40 in many protists, our study suggests that the mitochondrial disulfide relay evolved in a stepwise reaction from an Erv1-only system to which Mia40 was added in order to improve substrate specificity.Graphical AbstractThe mitochondrial disulfide relay evolved in a step-wise manner from an Erv1-only system.

【 授权许可】

CC BY   
© Herrmann et al. 2017