Abstract

Here we report the cloning and expression of αB-crystallin from the zebrafish. 5′- and 3′-RACE was used to isolate a 900-bp transcript that contained insertions and deletions that differentiate it from both αA-crystallin and HSP-27. The deduced amino acid sequence of zebrafish αB-crystallin revealed that it lacked four residues in the C-terminus implicated in protein–protein interactions in other vertebrate species. In addition, the sequence contained two substitutions at sites implicated in phosphorylation in other vertebrate species. Northern analysis and semi-quantitative RT-PCR indicate that zebrafish αB-crystallin is expressed at extremely low levels outside of the lens.

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