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Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase
Y Nakahashi1, S Taketani, M Okuda
1Third Department of Internal Medicine, Kansai Medical University, Osaka, Japan.
Biochemical and Biophysical Research Communications
|December 14, 1990
Summary
Researchers isolated the human ferrochelatase gene, crucial for heme synthesis. This discovery aids in understanding and potentially treating genetic disorders like erythropoietic protoporphyria.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Ferrochelatase (EC 4.99.1.1) is a key enzyme in heme biosynthesis.
- Understanding the human ferrochelatase gene is vital for studying related metabolic disorders.
Purpose of the Study:
- To isolate and characterize the cDNA encoding human ferrochelatase.
- To provide a basis for molecular analysis of ferrochelatase-related diseases.
Main Methods:
- Screening a human placenta cDNA library using a mouse ferrochelatase cDNA probe.
- DNA sequencing and Northern blot analysis to determine gene structure and expression.
Main Results:
- Isolated a 1269 bp cDNA encoding human ferrochelatase (423 amino acids).
- Mature protein identified as 369 amino acids; 88% sequence identity with mouse and 46% with yeast ferrochelatase.
- Detected two ferrochelatase mRNA transcripts (2500 and 1600 bp) in K562 and HepG2 cells.
Conclusions:
- The full-length human ferrochelatase cDNA has been successfully isolated.
- This molecular tool will facilitate the characterization of genetic defects in erythropoietic protoporphyria.