Cmc1p Is a Conserved Mitochondrial Twin CX9C Protein Involved in Cytochrome c Oxidase Biogenesis

• DOI: 10.1128/mcb.01920-07
• Publication Date: 2008-04-29T00:45:28Z
• Authors: Darryl Horn; Hassan Al-Ali; Antoni Barrientos
• Keywords: Chaperone (clinical); Intermembrane space; Mitochondrial intermembrane space; Conserved sequence; Mitochondrial matrix

Copper is an essential cofactor of two mitochondrial enzymes: cytochrome c oxidase (COX) and Cu-Zn superoxide dismutase (Sod1p). incorporation into these enzymes facilitated by metallochaperone proteins which probably use copper from a matrix-localized pool. Here we describe novel conserved metallochaperone-like protein, Cmc1p, whose function affects both COX Sod1p. In Saccharomyces cerevisiae, Cmc1p localizes to the inner membrane facing intermembrane space. for full expression respiration, contains twin CX9C domain in other assembly chaperones, has ability bind copper(I). Additionally, mutant cmc1 cells display increased Sod1p activity, while CMC1 overexpression results decreased activity. Our suggest that could play direct or indirect role trafficking distribution