Cmc1p is a conserved mitochondrial twin CX9C protein involved in cytochrome c oxidase biogenesis.

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 chaperones, 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.

journal_name

Mol Cell Biol

authors

Horn D,Al-Ali H,Barrientos A

doi

10.1128/MCB.01920-07

subject

Has Abstract

pub_date

2008-07-01 00:00:00

pages

4354-64

issue

13

eissn

0270-7306

issn

1098-5549

pii

MCB.01920-07

journal_volume

28

pub_type

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