Mitochondrial sulphydryl oxidase Erv1: both shuttle cysteine residues are required for its function with distinct roles

In this study, using yeast genetic approaches we showed that both shuttle cysteine residues of Erv1 are required for cell growth. In organelle and in vitro studies confirmed that both shuttle cysteines were indeed required for import of MIA-pathway substrates and Erv1 enzyme function to oxidise Mia40. Furthermore, our results revealed that the two shuttle cysteines of Erv1 are functionally distinct. While Cys33 is essential for forming the intermediate disulphide Cys33-Cys130’ and transferring electrons to the redox active-site directly, Cys30 plays two important roles: (i) dominantly interacts and receives electrons from Mia40 CPC, and (ii) resolves the Erv1 Cys33-Cys130 intermediate disulphide. Taken together, we conclude that both shuttle cysteines are required for Erv1 function, and play complementary but distinct roles to ensure rapid turnover of active Erv1.

Source: BJ Energy - March 13, 2014 Category: Biochemistry Authors: S Ang, M Zhang, T Lodi, H Lu Tags: BJ Biomolecules Source Type: research