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Phenylalanine hydroxylase gene: silent mutation uncovers evolutionary origin of different alleles
Author(s) -
Dworniczak Bernd,
AulehlaScholz Christa,
Horst Jürgen
Publication year - 1990
Publication title -
clinical genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 102
eISSN - 1399-0004
pISSN - 0009-9163
DOI - 10.1111/j.1399-0004.1990.tb03580.x
Subject(s) - phenylalanine hydroxylase , genetics , haplotype , allele , transition (genetics) , biology , gene , exon , mutant , mutation , complementary dna , point mutation , microbiology and biotechnology , amino acid , phenylalanine
Analyzing a panel of 94 phenylketonuria (PKU) alleles for mutations within the phenylalanine hydroxylase (PAH) gene, we identified a G to A transition in exon 7 corresponding to nucleotide 957 in the cDNA sequence. This nucleotide substitution generates a new Alu I site (…GTGGCT…→…GTAGCT…), but does not change the encoded amino acid (GTG 245 →GTA 245 = VAL). In our panel of patients the Alu I polymorphism is exclusively associated with haplotypes 4 (mutant or normal alleles) and 3, 16, 17, 28 (normal alleles).