Cloning of Murine Ferrochelatase
Overview
Authors
Affiliations
Ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1) catalyzes the last step in the heme biosynthetic pathway, the chelation of ferrous iron and protoporphyrin to form heme. The activity of ferrochelatase is deficient in the inherited disease protoporphyria. In this study, murine ferrochelatase cDNAs were obtained by screening cDNA libraries with an oligonucleotide probe. The derived amino acid sequence of murine ferrochelatase has 47% identity with the recently cloned Saccharomyces cerevisiae ferrochelatase, but it is not significantly similar to other published sequences. Results of Southern blotting are consistent with a single murine ferrochelatase gene, while Northern blotting demonstrates two ferrochelatase transcripts in all tissues examined. The ferrochelatase protein and mRNAs have different relative concentrations in different tissues. The cloning of murine ferrochelatase cDNAs provides the basis for future studies on ferrochelatase gene expression and on the identification of the molecular defect in protoporphyria.
Leung Y, Wong K, Lee H, Ho J Mol Cell Biochem. 2004; 262(1-2):225-31.
PMID: 15532727 DOI: 10.1023/b:mcbi.0000038238.27488.9f.
Expression of ferrochelatase mRNA in erythroid and non-erythroid cells.
Chan R, Schulman H, Ponka P Biochem J. 1993; 292 ( Pt 2):343-9.
PMID: 8503869 PMC: 1134215. DOI: 10.1042/bj2920343.
Analysis of the Bradyrhizobium japonicum hemH gene and its expression in Escherichia coli.
Frustaci J, Obrian M Appl Environ Microbiol. 1993; 59(8):2347-51.
PMID: 8368826 PMC: 182289. DOI: 10.1128/aem.59.8.2347-2351.1993.
Structure and function of ferrochelatase.
Ferreira G, Franco R, Lloyd S, Moura I, Moura J, Huynh B J Bioenerg Biomembr. 1995; 27(2):221-9.
PMID: 7592569 DOI: 10.1007/BF02110037.
Furukawa T, Kohno H, Tokunaga R, Taketani S Biochem J. 1995; 310 ( Pt 2):533-8.
PMID: 7544575 PMC: 1135927. DOI: 10.1042/bj3100533.