Proteobacteria-like ferrochelatase in the malaria parasite.
A gene encoding the heme biosynthetic enzyme ferrochelatase (FC) was found in the genomic DNA databases of Plasmodium spp. The predicted amino acid sequence of malarial FC is highly conserved and fairly well conserved by comparison with other orthologues. The FC genes of P. falciparum and P. yoelii are transcribed and the mRNAs are processed to encode polypeptides of the expected amino acid sequence. The cloned cDNA for the FC of P. falciparum successfully rescued a FC-null mutant of Escherichia coli, indicating that it encodes an active enzyme. Unlike eukaryotic FCs, the malarial enzyme lacks a characteristic extension at the C-terminus. In addition, the sequence of the malarial FC resembles proteobacterial orthologues rather than eukaryotic enzymes. Strikingly, the malarial FC lacks a bipartite presequence at its N-terminus, unlike delta-aminolevulinic acid dehydratase of the same organism. This suggests an unusual intracellular distribution of heme biosynthetic enzymes, involving multiple subcellular compartments.
Sato
Shigeharu
S
Division of Parasitology, National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK. ssato@nimr.mrc.ac.uk
Wilson
R J M
RJ
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D017931:DNA Primers; D005294:Ferrochelatase / Q000235:genetics*; D015971:Gene Expression Regulation, Enzymologic; D005816:Genetic Complementation Test; D014644:Genetic Variation; D007438:Introns; D008969:Molecular Sequence Data; D010802:Phylogeny; D010963:Plasmodium falciparum / Q000145:classification / Q000201:enzymology / Q000235:genetics*; D016133:Polymerase Chain Reaction; D020560:Proteobacteria / Q000145:classification / Q000201:enzymology / Q000235:genetics*; D020133:Reverse Transcriptase Polymerase Chain Reaction; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014158:Transcription, Genetic
D017931:DNA Primers; D005294:Ferrochelatase