Abstract
Uroporphyrinogen decarboxylase, the fifth enzyme of the heme biosynthetic pathway, is an housekeeping enzyme whose activity is enhanced during erythropoietic differentiation. We have previously shown that this increased activity was in part accounted for by an enhanced transcription of the gene in erythropoietic tissues. To elucidate further the tissue specific regulation of an housekeeping gene we have isolated the human URO-D gene and determined its organization. The cloned gene comprises 10 exons spread over 3 Kb. Two transcriptional start sites were determined and analysis of 900 bp of the 5' flanking region suggests a very simple structural organization for the URO-D gene promoter. We also show that this gene is functional when transfected into mouse fibroblasts, and that its promoter is sensitive to a viral enhancer.
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