Abstract
Complete deficiency of hypoxanthine-guanine phosphoribosyl-transferase (HPRT) causes Lesch-Nyhan syndrome. We have identified the mutation in a cDNA clone encoding HPRTYale, isolated from a subject with Lesch-Nyhan syndrome. This mutant enzyme is characterized by normal mRNA and protein concentrations, no residual catalytic activity and cathodal migration in polyacrylamide gel electrophoresis. We have cloned and sequenced a full-length cDNA (1378bp) from cultured lymphoblasts derived from the subject HPRTYale. A single nucleotide change (G→C) has been identified in its coding region. This transversion predicts an amino acid substitution from glycine (GGC) to arginine (CGC) in codon 71, explaining the cathodal migration of HPRTYale. Inclusion of the bulky arginine side chain in place of glycine probably disrupts protein folding.
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