Sequence and spatial expression of zebrafish (Danio rerio) alphaA-crystallin

Mol Vis. 2002 Mar 11;8:45-50.

Abstract

Purpose: To determine the nucleotide sequence, amino acid sequence and tissue specificity of zebrafish alphaA-crystallin.

Methods: RACE, both 3' and 5', was used to clone the zebrafish alphaA-crystallin gene. The peptide sequence of the encoded protein was deduced and compared to cavefish, shark, amphibian, bird and human orthologues using the CLUSTAL W algorithm. alphaA-crystallin transcript was evaluated in brain, heart, lens, liver, skeletal muscle/skin, and spleen by semi-quantitative RT-PCR.

Results: The 173 amino acid sequence of zebrafish alphaA-crystallin was determined to be 73% and 86% similar to its human and cavefish orthologues, respectively. We detected high expression of zebrafish alphaA-crystallin in the lens and very low expression in liver and spleen.

Conclusions: Few amino acids identified as being functionally important to chaperone function differ between zebrafish and mammalian alphaA-crystallin. The expression of alphaA-crystallin is mainly confined to the lens in both taxa. These data suggest that zebrafish alphaA-crystallin plays a physiologically limited role outside of the zebrafish lens, similar to its mammalian orthologues.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Crystallins / genetics*
  • Crystallins / isolation & purification
  • Crystallins / metabolism
  • Gene Expression Regulation
  • Humans
  • Lens, Crystalline / chemistry
  • Lens, Crystalline / metabolism
  • Molecular Sequence Data
  • RNA, Messenger / analysis
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Homology, Amino Acid
  • Zebrafish / genetics*

Substances

  • Crystallins
  • RNA, Messenger