Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification
| Autor: | Philippe Goyette, Rima Rozen, Rowena G. Matthews, David S. Rosenblatt, Renate Milos, Alessandra M.V. Duncan, James S. Sumner |
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| Rok vydání: | 1994 |
| Předmět: |
Male
DNA Complementary Methylenetetrahydrofolate reductase deficiency Swine Nonsense mutation Molecular Sequence Data Biology Bacterial Proteins Complementary DNA Genetics medicine Missense mutation Animals Humans Point Mutation Amino Acid Sequence Peptide sequence Homocysteine Methylenetetrahydrofolate Reductase (NADPH2) Oxidoreductases Acting on CH-NH Group Donors Base Sequence Sequence Homology Amino Acid Point mutation Nucleic acid sequence Chromosome Mapping medicine.disease digestive system diseases Pedigree Cardiovascular Diseases Chromosomes Human Pair 1 Methylenetetrahydrofolate reductase biology.protein Female Nervous System Diseases |
| Zdroj: | Nature genetics. 7(2) |
| ISSN: | 1061-4036 |
| Popis: | Methylenetetrahydrofolate reductase (MTHFR) catalyses the reduction of methylenetetrahydrofolate to methyltetrahydrofolate, a cofactor for homocysteine methylation to methionine. MTHFR deficiency, an autosomal recessive disorder, results in homocysteinemia. Using degenerate oligonucleotides based on porcine peptide sequence data, we isolated a 90-bp cDNA by PCR from pig liver RNA. This cDNA was used to isolate a human cDNA, the predicted amino acid sequence of which shows strong homology to porcine MTHFR and to bacterial metF genes. The human gene has been localized to chromosome 1p36.3. Two mutations were identified in MTHFR-deficient patients: a missense mutation (Arg to Gln), in a residue conserved in bacterial enzymes, and a nonsense mutation (Arg to Ter). |
| Databáze: | OpenAIRE |
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