THE ISOLATION AND CHARACTERIZATION OF A DROSOPHILA GENE ENCODING A PUTATIVE NAD-DEPENDENT METHYLENETETRAHYDROFOLATE DEHYDROGENASE-METHENYLTETRAHYDROFOLATE CYCLOHYDROLASE
Bd. Price et A. Laughon, THE ISOLATION AND CHARACTERIZATION OF A DROSOPHILA GENE ENCODING A PUTATIVE NAD-DEPENDENT METHYLENETETRAHYDROFOLATE DEHYDROGENASE-METHENYLTETRAHYDROFOLATE CYCLOHYDROLASE, Biochimica et biophysica acta, 1173(1), 1993, pp. 94-98
Mammalian NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase-5
,10-methenyltetrahydrofolate cyclohydrolase is a bifunctional mitochon
drial enzyme expressed in most established cell lines but only in deve
loping normal tissues. We report the cloning and molecular characteriz
ation of a Drosophila gene (DNMDMC) that encodes a protein with 56% id
entity to the mammalian bifunctional protein. Like the mammalian bifun
ctional proteins, the Drosophila protein contains a putative mitochond
rial targeting sequence and its transcripts are expressed in developin
g 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 ge
nes.