Editing of human alpha-galactosidase RNA resulting in a pyrimidine to purine conversion

During a study of the gene coding for alpha-galactosidase (EC 3.2.1.22), the lysosomal enzyme deficient in Fabry's disease, RT-PCR amplification of alpha-galactosidase mRNAs obtained from three different tissues isolated from males revealed a substantial number of clones with a U to A conversio...

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Bibliographic Details
Published in:Nucleic acids research 1995-07, Vol.23 (14), p.2636-2640
Main Authors: Novo, F J, Kruszewski, A, MacDermot, K D, Goldspink, G, Górecki, D C
Format: Article
Language:English
Subjects:
alpha-Galactosidase - genetics
Base Sequence
Deoxyribonucleases, Type II Site-Specific
DNA Primers - genetics
DNA, Complementary - chemistry
DNA, Complementary - genetics
Humans
Male
Molecular Sequence Data
Nucleic Acid Conformation
Polymerase Chain Reaction
RNA Editing - genetics
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Summary:During a study of the gene coding for alpha-galactosidase (EC 3.2.1.22), the lysosomal enzyme deficient in Fabry's disease, RT-PCR amplification of alpha-galactosidase mRNAs obtained from three different tissues isolated from males revealed a substantial number of clones with a U to A conversion at the nucleotide position 1187. Such a modification of the coding sequence would result in an amino acid substitution in the C-terminal region (Phe396Tyr) of the enzyme. Neither PCR analysis of the genomic sequence nor the RT-PCR amplification of RNA obtained by in vitro transcription of the wild-type cDNA showed this change in the sequence. Multiple genes, pseudogenes are allelic variants were excluded. Hence, we propose RNA editing as a mechanism responsible for this base change in the alpha-galactosidase RNA.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/23.14.2636