Disease relevance of ARH1

• We demonstrate the capacity of recombinant Arh1p, made in Escherichia coli, to substitute for its mammalian homologue in ferricyanide, cytochrome c reduction, and, more importantly, in vitro 11beta-hydroxylase assays [1].

High impact information on ARH1

• Adrenodoxin reductase homolog (Arh1p) of yeast mitochondria required for iron homeostasis [2].
• Finally, a time course correlated the cellular depletion of Arh1p with the coordinated appearance of various mutant phenotypes including dysregulated cellular iron uptake, deficiency of Fe-S protein activities in mitochondria and cytoplasm, and deficiency of hemoproteins [2].
• Consequently ARH1p joins the small group of gene products that affect essential functions carried out by the organelle and not linked to oxidative phosphorylation [3].
• In the first part of this article, we use structural bioinformatics methods to evaluate the possibility of interaction between Arh1 and Yah1 [4].
• The predicted complex allows us to suggest point mutations to either molecule that could hinder Arh1-Yah1 interaction and test the role of Arh1 as the reductase for Yah1 [4].

Anatomical context of ARH1

• The previous identification of a homolog of the first mammalian enzyme in yeast, ARH1, also shown to be essential (Manzella, L., Barros, M.H., Nobrega, F.G., 1998. Yeast 14, 839-846), strongly suggests that there is a novel electron transfer chain, unlinked to respiration, and of essential function in mitochondria [5].

References