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Issue 12, 2010
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Genome-wide analysis of eukaryotic twin CX9C proteins

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Twin CX9C proteins are eukaryotic proteins that derive their name from their characteristic motif, consisting of two pairs of cysteines that form two disulfide bonds stabilizing a coiled coil–helix–coiled coil–helix (CHCH) fold. The best characterized of these proteins are Cox17, a copper chaperone acting in cytochrome c oxidase biogenesis, and Mia40, the central component of a system for protein import into the mitochondrial inter-membrane space (IMS). However, the range of possible functions for these proteins is unclear. Here, we performed a systematic search of twin CX9C proteins in eukaryotic organisms, and classified them into groups of putative homologues, by combining bioinformatics methods with literature analysis. Our results suggest that the functions of most twin CX9C proteins vary around the common theme of playing a scaffolding role, which can tie their observed roles in mitochondrial structure and function. This study will enhance the present annotation of eukaryotic proteomes, and will provide a rational basis for future experimental work aimed at a deeper understanding of this remarkable class of proteins.

Graphical abstract: Genome-wide analysis of eukaryotic twin CX9C proteins

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Publication details

The article was received on 18 Jun 2010, accepted on 01 Sep 2010 and first published on 04 Oct 2010

Article type: Paper
DOI: 10.1039/C0MB00058B
Citation: Mol. BioSyst., 2010,6, 2459-2470
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    Genome-wide analysis of eukaryotic twin CX9C proteins

    G. Cavallaro, Mol. BioSyst., 2010, 6, 2459
    DOI: 10.1039/C0MB00058B

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