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J. Biol. Chem., Vol. 277, Issue 1, 656-664, January 4, 2002

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Structure and Expression of the Scallop -Crystallin Gene
EVIDENCE FOR CONVERGENT EVOLUTION OF PROMOTER SEQUENCES^*

Eleonora Carosa^§, Zbynek Kozmik, J. Edward Rall^¶, and Joram Piatigorsky

From the  Laboratory of Molecular and Developmental Biology, National Eye Institute and the ^¶ Diabetes Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892

-Crystallin of the scallop lens is an inactive aldehyde dehydrogenase (1A9). Here we have cloned the scallop -crystallin gene. Except for an extra novel first exon, its 14-exon structure agrees well with that of mammalian aldehyde dehydrogenases 1, 2, and 6. The 2120/+63, 714/+63, and 156/+63 -crystallin promoter fragments drive the luciferase reporter gene in transfected TN4-1 lens cells and L929 fibroblasts but not in Cos7 cells. Putative binding sequences for cAMP-responsive element-binding protein (CREB)/Jun, ACRYBP1, AP-1, and PAX-6 in the -crystallin promoter are surprisingly similar to the cis-elements used for lens promoter activity of the mouse and chicken A-crystallin genes, which encode proteins homologous to small heat shock proteins. Site-specific mutations in the overlapping CREB/Jun and Pax-6 sites abolished activity of the -crystallin promoter in transfected cells. Gel shift experiments utilizing extracts from the TN4-1, L929, and Cos7 cells and the scallop stomach and oligonucleotides derived from the putative binding sites of the -crystallin promoter showed complex formation. Gel shift experiments showed binding of recombinant Pax-6 and CREB to their respective sites. Our data suggest convergent evolutionary adaptations that underlie the preferential expression of crystallin genes in the lens of vertebrates and invertebrates.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AF175578.

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