The isolation and characterization of a Drosophila gene encoding a putative NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase.
Mammalian NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase-5,10-methenyltetrahydrofolate cyclohydrolase is a bifunctional mitochondrial enzyme expressed in most established cell lines but only in developing normal tissues. We report the cloning and molecular characterization of a Drosophila gene (DNMDMC) that encodes a protein with 56% identity to the mammalian bifunctional protein. Like the mammalian bifunctional proteins, the Drosophila protein contains a putative mitochondrial targeting sequence and its transcripts are expressed in developing tissues. Unlike its mammalian homologs, DNMDMC is expressed at high levels in adult tissues. DNMDMC maps to polytene chromosome band 85C, is encoded in three exons, and is closely flanked by two additional genes.
Price
B D
BD
Laboratory of Genetics, University of Wisconsin, Madison 53706.
Laughon
A
A
D000595:Amino Acid Sequence; D000619:Aminohydrolases / Q000235:genetics*; D000818:Animals; D001483:Base Sequence; D004330:Drosophila / Q000235:genetics*; D005260:Female; D006801:Humans; D008297:Male; D008754:Methylenetetrahydrofolate Dehydrogenase (NADP) / Q000235:genetics*; D051379:Mice; D008928:Mitochondria / Q000201:enzymology; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000235:genetics*; D009243:NAD / Q000378:metabolism; D016415:Sequence Alignment
D009097:Multienzyme Complexes; C055342:methylene tetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase; D009243:NAD; D008754:Methylenetetrahydrofolate Dehydrogenase (NADP); D000619:Aminohydrolases