Phenylalanine hydroxylase gene: silent mutation uncovers evolutionary origin of different alleles
- 1 October 1990
- journal article
- research article
- Published by Wiley in Clinical Genetics
- Vol. 38 (4) , 270-273
- https://doi.org/10.1111/j.1399-0004.1990.tb03580.x
Abstract
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... .fwdarw. ...GTAGCT...), but does not change the encoded amino acid (GTG245 .fwdarw. GTA245 = 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).Keywords
This publication has 7 references indexed in Scilit:
- A BETA-THALASSEMIA GENE CAUSED BY A 290-BASE PAIR DELETION - ANALYSIS BY DIRECT SEQUENCING OF ENZYMATICALLY AMPLIFIED DNA1989
- A beta-thalassemia gene caused by a 290-base pair deletion: analysis by direct sequencing of enzymatically amplified DNABlood, 1989
- Phenylketonuria: distribution of DNA diagnostic patterns in German familiesHuman Genetics, 1988
- The CpG dinucleotide and human genetic diseaseHuman Genetics, 1988
- Meiotic recombination between two polymorphic restriction sites within the beta globin gene cluster.Journal of Medical Genetics, 1986
- EXTENSIVE RESTRICTION SITE POLYMORPHISM AT THE HUMAN PHENYLALANINE-HYDROXYLASE LOCUS AND APPLICATION IN PRENATAL-DIAGNOSIS OF PHENYLKETONURIA1985
- Nucleotide sequence of a full-length complementary DNA clone and amino acid sequence of human phenylalanine hydroxylaseBiochemistry, 1985