Cloning and sequencing of a cDNA for human mitochondrial ubiquinone-binding protein of complex III.
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Suzuki H, Hosokawa Y, Toda H, Nishikimi M, Ozawa T
Cloning and sequencing of a cDNA for human mitochondrial ubiquinone-binding protein of complex III.
Biochem Biophys Res Commun. 1988 Oct 31;156(2):987-94.
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- 3056408 [ View in PubMed]
- Abstract
The ubiquinone-binding protein (QP-C) is a nuclear-encoded component of ubiquinol-cytochrome c oxidoreductase in the mitochondrial respiratory chain and plays an important role in electron transfer as a ubiquinone-QP-C complex. We obtained a partial cDNA for rat liver QP-C by screening a lambda gt11 rat liver cDNA library using antiserum directed against bovine heart QP-C. Using this cDNA as a probe, a cDNA clone was isolated from a human fibroblast cDNA library by colony hybridization. The total length of the cloned cDNA was 518 base pairs with an open reading frame of 333 base pairs. The 111-amino acid sequence deduced from the nucleotide sequence of the cDNA is 85% homologous to that of bovine QP-C and contains only a single additional amino-terminal methionine. This implies that the human QP-C is synthesized without a presequence which is required for import of most nuclear-encoded mitochondrial proteins into mitochondria.