Autosomal albino chicken mutation (ca/ca) deletes hexanucleotide (-deltaGACTGG817) at a copper-binding site of the tyrosinase gene
| Autor: | T. Tobita-Teramoto, K. Kino, D. W. Salter, G. Y. Jang, Toyoko Akiyama, John A. Brumbaugh |
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| Rok vydání: | 2000 |
| Předmět: |
DNA
Complementary Tyrosinase Molecular Sequence Data Biology medicine.disease_cause chemistry.chemical_compound Complementary DNA Aspartic acid medicine Animals Point Mutation Amino Acid Sequence RNA Messenger Gene Cells Cultured chemistry.chemical_classification Mutation Binding Sites Base Sequence Monophenol Monooxygenase Reverse Transcriptase Polymerase Chain Reaction Point mutation General Medicine Sequence Analysis DNA Molecular biology Amino acid chemistry Biochemistry Melanocytes Animal Science and Zoology Chickens DNA Copper Gene Deletion |
| Zdroj: | Poultry science. 79(1) |
| ISSN: | 0032-5791 |
| Popis: | We compared tyrosinase cDNA sequences from a line of autosomal albino and Black Silky chickens isolated from cultured melanocytes by reverse transcription-polymerase chain reaction (RT-PCR). Both sources produce a single DNA fragment of predicted normal tyrosinase size. Direct sequencing of the PCR product showed three mutated sites in the tyrosinase gene of the albino chicken. Two silent point mutations and a deletion of six nucleotides (-ΔGACTGG) at 817 bp in the tyrosinase cDNA sequence were observed when compared with the White Leghorn and Black Silky cDNA sequences. The deduced albino chicken tyrosinase protein lacks two amino acids, aspartic acid and tryptophan. The position of these amino acids is consistent with one of the potential copper-binding sites that should be indispensable for function of the enzyme. We speculate that the six-base deletion is responsible for the inactive tyrosinase in this line of albino chickens. |
| Databáze: | OpenAIRE |
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