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ZFIN ID: ZDB-PUB-020403-14
Sequence and spatial expression of zebrafish (Danio rerio) alphaA-crystallin
Runkle, S., Hill, J., Kantorow, M., Horwitz, J., and Posner, M.
Date: 2002
Source: Molecular Vision   8: 45-50 (Journal)
Registered Authors: Posner, Mason
Keywords: none
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*
PubMed: 11925526
ABSTRACT
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.
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