A-crystallin binding protein I (A-CRYBP1) is a ubiquitously expressed DNA binding protein that was previously identified by its ability to interact with a functionally important sequence in the mouse A-crystallin gene promoter. Here, we have cloned a single copy gene with 10 exons spanning greater than 70 kb of genomic DNA that encodes A-CRYBP1. The mouse A-CRYBP1 gene specifies a 2,688-amino acid protein with 72% amino acid identity to its human homologue, PRDII-BF1. Both the human and the mouse proteins contain two sets of consensus CH zinc fingers at each end as well a central nonconsensus zinc finger. The A-CRYBP1 gene produces a 9.5-kb transcript in 11 different tissues as well as a testis-specific, 7.7-kb transcript. A-CRYBP1 cDNA clones were isolated from adult mouse brain and testis as well as from cell lines derived from mouse lens (TN4-1) and muscle (CC). A single clone isolated from the muscle CC library contains an additional exon near the 5`-end that would prevent production of a functional protein if the normal translation start site were utilized; however, there is another potential initiation codon located downstream that is in frame with the rest of the coding region. In addition, we identified multiple cDNAs from the testis in which the final intron is still present. Finally, we used an antisense expression construct derived from an A-CRYBP1 cDNA clone to provide the first functional evidence that A-CRYBP1 regulates gene expression. When introduced into the TN4-1 mouse lens cell line, the antisense construct significantly inhibited expression from a heterologous promoter that utilized the A-CRYBP1 binding site as an enhancer.

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