---

Horn D, et al.  (2008) Cmc1p is a conserved mitochondrial twin CX9C protein involved in cytochrome c oxidase biogenesis. Mol Cell Biol 28(13):4354-64

Abstract: Copper is an essential cofactor of two mitochondrial enzymes: cytochrome c oxidase (COX) and Cu-Zn superoxide dismutase (Sod1p). Copper incorporation into these enzymes is facilitated by metallochaperone proteins which probably use copper from a mitochondrial matrix localized pool. Here we describe a novel conserved mitochondrial metallochaperone-like protein, Cmc1p, whose function affects both COX and Sod1p. In Saccharomyces cerevisiae, Cmc1p localizes to the mitochondrial inner membrane facing the intermembrane space. Cmc1p is essential for full expression of COX and respiration, contains a twin Cx9C domain conserved in other COX assembly copper chaperons and has the ability to bind copper(I). Additionally, mutant cmc1 cells display increased mitochondrial Sod1p activity while CMC1 overexpression results in decreased Sod1p activity. Our results suggest that Cmc1p could play a direct or indirect role in copper trafficking and distribution to COX and Sod1p.

Status: Published

Type: Journal Article

PubMed ID: 18443040

---

Author Searches

To find contact information or other publications by the authors of this paper, follow these three steps:

1. (1) Choose an author,
2. (2) Choose a search parameter,
3. (3) Click to implement

Horn D Al-Ali H Barrientos A Papers in SGD Colleagues in SGD PubMed Google Scholar

---