J1-crystallins of the cubomedusan jellyfish lens constitute a novel family encoded in at least three intronless genes.

The transparent cellular eye lens of the jellyfish (Tripedalia cystophora) contains three major proteins called J1-, J2-, and J3-crystallins. Here we have isolated cDNAs encoding three novel 37-kDa J1-crystallin polypeptides (J1A, J1B, and J1C) sharing 84-98% identity in amino acid sequence among themselves. Each polypeptide is encoded in a separate gene lacking introns. In contrast to the striking similarity of the coding regions, the 5'- and 3'-untranslated sequences of the three J1-crystallin mRNAs are completely different, consistent with an ancient duplication of their genes. Thermostability experiments showed that J1-crystallins remain soluble at 50 degrees C, but precipitate at 60 degrees C, suggesting that these major lens proteins are neither heat shock proteins nor unusually heat-resistant as are many vertebrate crystallins. Although J1 mRNAs appear polyadenylated, no typical polyadenylation signal was detected in the cDNAs. Surprisingly, the only obvious similarities among the 5'-flanking regions of the three J1-crystallin genes are putative TATA boxes and several CAAT sequences, consistent with fewer evolutionary constraints on the regulatory sequences than on the coding sequences of these crystallin genes.