Molecular cloning and nucleotide sequence of a complete human uroporphyrinogen decarboxylase cDNA
Roméo, P H × Raich, N Dubart, A Beaupain, D Pryor, M Kushner, J Cohen-Solal, M Goossens, Marcel #
Journal of Biological Chemistry vol:261 issue:21 pages:9825-31
We have cloned and sequenced a full-length cDNA coding for human uroporphyrinogen decarboxylase. The deduced 367-amino acid sequence is consistent with the molecular weight, the partial amino acid sequence of cyanogen bromide peptides, and the total amino acid composition of the purified enzyme. Southern analysis of human genomic DNA shows that its gene is present as a single copy in the human genome, and Northern analysis demonstrates the presence of a single size species of mRNA in erythroid and non-erythroid tissues and in several cultured cell lines. We have also demonstrated that the level of uroporphyrinogen decarboxylase mRNA is markedly increased in tissues or cell lines of erythroid origin and that this is due to a tissue-specific transcriptional activation of the uroporphyrinogen decarboxylase gene.