Cobine PA, et al. (2006) Mitochondrial matrix copper complex used in metallation of cytochrome oxidase and superoxide dismutase. J Biol Chem 281(48):36552-9
Abstract: A mitochondrial matrix copper ligand (CuL) complex, conserved in mammalian cells, is the likely source of copper for assembly of cytochrome c oxidase (CcO) and superoxide dismutase-1 (Sod1) within the intermembrane space (IMS) in yeast. Targeting the copper-binding proteins, human Sod1 and Crs5, to the mitochondrial matrix results in growth impairment on non-fermentable medium due to decreased levels of CcO. This effect is reversed by copper supplementation. Matrix-targeted Crs5 diminished Sod1 protein within the IMS and impaired activity of an inner membrane tethered hSod1. Copper binding by the matrix-targeted proteins attenuates levels of the CuL complex without affecting total mitochondrial copper. These data suggest that attenuation of the matrix CuL complex via heterologous competitors limits available copper for metallation of CcO and Sod1 within the IMS. The ligand also exists in the cytoplasm in an apparent metal-free state.
|Status: Published||Type: Journal Article||PubMed ID: 17008312|
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