Characterization of the human dihydropyrimidinase-related protein 2 (DRP-2) gene.

The genes within the dihydropyrimidinase-related protein (DRP) family, were originally identified in humans by their homology to dihydropyrimidinase (DHP). Four members of this gene family, DRP-1, -2, -3 and -4, are expressed mainly in the fetal and neonatal brains of mammals and chickens, and have been implicated as intracellular signal transducers in the development of the nervous system. We isolated the human DRP-2 gene, and determined its transcriptional start site and exon/intron organization. The gene spanned more than 62 kb, and contained 14 exons with lengths ranging from 62 bp to 2606 bp. The transcriptional start site was determined by an RNase protection assay and 5' rapid amplification of cDNA ends (RACE), and a highly GC-rich promoter was identified that contained possible regulatory elements such as a TATA box, CAAT box and three GC boxes. Comparison of the phase and position of intron insertions within the human DRP-2 gene with those within DRP-1, DHP and two Caenorhabditis elegans DRP/DHP homologs, indicated that DRPs are more conserved in their exon/intron organization than DHP.