Autosomal albino chicken mutation (ca/ca) deletes hexanucleotide (-deltaGACTGG817) at a copper-binding site of the tyrosinase gene

• Published in: Poultry science Vol. 79; no. 1; pp. 46 - 50
• Main Authors: Tobita-Teramoto, T, Jang, G Y, Kino, K, Salter, D W, Brumbaugh, J, Akiyama, T
• Format: Journal Article
• Language: English
• Published: England 01.01.2000
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cells, Cultured; Chickens - genetics; Copper - metabolism; DNA, Complementary - chemistry; Gene Deletion; Melanocytes - enzymology; Molecular Sequence Data; Monophenol Monooxygenase - genetics; Mutation; Point Mutation; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger - analysis; Sequence Analysis, DNA
• ISSN: 0032-5791
• DOI: 10.1093/ps/79.1.46

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 (-deltaGACTGG) 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.