Molecular cloning and biochemical analysis of tyrosinase from the crested ibis in China

Biochem Genet. 2012 Dec;50(11-12):936-45. doi: 10.1007/s10528-012-9533-1. Epub 2012 Sep 19.

Abstract

The crested ibis, one of the most endangered birds in the world, could benefit from research into its genetic diversity as a tool for conservation in the future. Tyrosinase is thought to play a major role in the production of common yellow to black melanins in birds. We have cloned and sequenced four exons of the crested ibis tyrosinase gene and discovered that the amino acid sequence has high similarity to zebra finch tyrosinase (93 %), followed by chicken (91 %) and quail (91 %). Some functional and structural domains in the crested ibis tyrosinase coding area were found to be conserved during evolution. Nine sequence variants were found in the partial coding sequence, one in exon 1 and eight in exon 4. Sequence variant 1 (SV1) shows intermediate polymorphism (0.25 < PIC < 0.5), and further study is needed to determine whether it can be used as a potential molecular marker in crested ibis artificial breeding programs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Avian Proteins / genetics*
  • Base Sequence
  • Binding Sites
  • Birds / genetics*
  • Chickens / genetics
  • China
  • Cloning, Molecular
  • Computational Biology
  • Conserved Sequence
  • Endangered Species
  • Evolution, Molecular
  • Exons
  • Gene Frequency
  • Genetic Markers
  • Heterozygote
  • Molecular Sequence Data
  • Monophenol Monooxygenase / chemistry*
  • Monophenol Monooxygenase / genetics
  • Polymorphism, Genetic
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid

Substances

  • Avian Proteins
  • Genetic Markers
  • Monophenol Monooxygenase