Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase.
The cDNA encoding human ferrochelatase [EC 4.99.1.1] was isolated from a human placenta cDNA library in bacteriophage lambda gt11 by screening with a radiolabeled fragment of mouse ferrochelatase cDNA. The cDNA had an open reading frame of 1269 base pairs (bp) encoding a protein of 423 amino acid residues (Mr. 47,833) with alternative putative polyadenylation signals in the 3' non-coding regions and poly (A) tails. Amino acid sequencing showed that the mature protein consists of 369 amino acid residues (Mr. 42,158) with a putative leader sequence of 54 amino acid residues. The human enzyme showed an 88% identity to mouse enzyme and 46% to yeast enzyme. Northern blot analysis showed two mRNAs of about 2500 and 1600 bp for ferrochelatase in K562 and HepG2 cells. As full-length cDNA for human ferrochelatase is now available, molecular lesions related to erythropoietic protoporphyria can be characterized.
Nakahashi
Y
Y
Third Department of Internal Medicine, Kansai Medical University, Osaka, Japan.
Taketani
S
S
Okuda
M
M
Inoue
K
K
Tokunaga
R
R
D000595:Amino Acid Sequence; D000818:Animals; D015152:Blotting, Northern; D002417:Cattle; D003001:Cloning, Molecular; D004247:DNA / Q000096:biosynthesis*; D005294:Ferrochelatase / Q000096:biosynthesis / Q000235:genetics*; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D012333:RNA, Messenger / Q000737:chemistry; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D014407:Tumor Cells, Cultured
D012333:RNA, Messenger; D004247:DNA; D005294:Ferrochelatase