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Closed Access item A Mutation in Para-Hydroxybenzoate-Polyprenyl Transferase (COQ2) Causes Primary Coenzyme Q10 Deficiency

Authors:Quinzii, Catarina
Naini, Ali
Salviati, Leonardo
Trevisson, Eva
Navas, Plácido
DiMauro, Salvatore
Hirano, Michio
Keywords:Coenzyme Q10, Cysteine, Tyrosine, Alkyl and Aryl Transferases, Fibroblasts, Mitochondrial encephalomyopathies, Ubiquinone, 4-hydroxybenzoate polyprenyltransferase
Issue Date:Feb-2006
American Society of Human Genetics
Citation:American Journal of Human Genetics 78(2): 345-349 (2006)
Abstract:Ubiquinone (coenzyme Q10 or CoQ10) is a lipid-soluble component of virtually all cell membranes, where it functions as a mobile electron and proton carrier. CoQ10 deficiency is inherited as an autosomal recessive trait and has been associated with three main clinical phenotypes: a predominantly myopathic form with central nervous system involvement, an infantile encephalomyopathy with renal dysfunction, and an ataxic form with cerebellar atrophy. In two siblings of consanguineous parents with the infantile form of CoQ10 deficiency, we identified a homozygous missense mutation in the COQ2 gene, which encodes para-hydroxybenzoate-polyprenyl transferase. The A→G transition at nucleotide 890 changes a highly conserved tyrosine to cysteine at amino acid 297 within a predicted transmembrane domain. Radioisotope assays confirmed a severe defect of CoQ10 biosynthesis in the fibroblasts of one patient. This mutation in COQ2 is the first molecular cause of primary CoQ10 deficiency.
Description:5 páginas, 2 figuras, 1 tabla.
Publisher version (URL):http://dx.doi.org/10.1086/500092
E-ISSNmetadata.dc.identifier.doi = DOI:1537-6605
Appears in Collections:(CABD) Artículos

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