Abstract
A full-length chicken delta-crystallin cDNA (p delta Cr17) was cloned and subjected to sequence analysis. The cDNA was shown to be full-length by both primer extension and S1 and mung bean nuclease experiments. Thus, the complete amino acid sequence of delta-crystallin is now available. The delta-crystallin polypeptide has a molecular mass of 48,542 daltons, as expected from its behavior on NaDodSO4/polyacrylamide gels. delta-Crystallin has one tryptophan, no cysteines, a prevalence of leucines (15%), and a paucity of aromatic residues. High alpha-helical content throughout the protein was predicted from the amino acid sequence. Nucleic acid sequence analysis suggests that delta-crystallin gene 1 encodes the mRNA that gave rise to the cDNA clone. These data provide a basis for the detailed analysis of the two delta-crystallin genes.
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