Journal
GENOMICS
Volume 70, Issue 2, Pages 223-231Publisher
ACADEMIC PRESS INC
DOI: 10.1006/geno.2000.6373
Keywords
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Funding
- NCRR NIH HHS [2 M01 RR00071] Funding Source: Medline
- NICHD NIH HHS [5 P30 HD28822] Funding Source: Medline
- NIDDK NIH HHS [5 R01 DK26824] Funding Source: Medline
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Uroporphyrinogen-III (URO) synthase is the heme biosynthetic enzyme defective in congenital erythropoietic porphyria. The similar to 34-kb human URO-synthase gene (UROS) was isolated, and its organization and tissue-specific expression were determined. The gene had two promoters that generated housekeeping and erythroid-specific transcripts with unique 5'-untranslated sequences (exons 1 and 2A) followed by nine common coding exons (2B to 10). Expression arrays revealed that the housekeeping transcript was present in all tissues, while the erythroid transcript was only in erythropoietic tissues. The housekeeping promoter lacked TATA and SP1 sites, consistent with the observed low level expression in most cells, whereas the erythroid promoter contained GATA1 and NF-ES sites for erythroid specificity. Luciferase reporter assays demonstrated that the housekeeping promoter was active in both erythroid K562 and HeLa cells, while the erythroid promoter was active only in erythroid cells and its activity was increased during hemin-induced erythroid differentiation. Thus, human URO-synthase expression is regulated during erythropoiesis by an erythroid-specific alternative promoter. (C) 2000 Academic Press.
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