Autosomal albino chicken mutation (ca/ca) deletes hexanucleotide (-ΔGACTGG817) at a copper-binding site of the tyrosinase gene

T. Tobita-Teramoto, G. Y. Jang, K. Kino, D. W. Salter, J. Brumbaugh, T. Akiyama

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)46-50
Number of pages5
JournalPoultry Science
Volume79
Issue number1
DOIs
Publication statusPublished - 2000 Jan

Keywords

  • Albino
  • Chicken
  • Copper-binding site
  • Mutation
  • Tyrosinase

ASJC Scopus subject areas

  • Animal Science and Zoology

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