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J Biol Chem, Vol. 273, Issue 15, 9249-9254, April 10, 1998
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From the Dolichol-phosphate-mannose (Dol-P-Man) serves as
a donor of mannosyl residues in major eukaryotic glycoconjugates. It
donates four mannosyl residues in the N-linked
oligosaccharide precursor and all three mannosyl residues in the core
of the glycosylphosphatidylinositol anchor. In yeasts it also donates
one mannose to the O-linked oligosaccharide. The yeast
DPM1 gene encodes a Dol-P-Man synthase that is a
transmembrane protein expressed in the endoplasmic reticulum. We cloned
human and mouse homologues of DPM1, termed
hDPM1 and mDPM1, respectively, both of which
encode proteins of 260 amino acids, having 30% amino acid identity
with yeast Dpm1 protein but lacking a hydrophobic transmembrane domain,
which exists in the yeast synthase. Human and mouse DPM1
cDNA restored Dol-P-Man synthesis in mouse Thy-1-deficient mutant
class E cells. Mouse class E mutant cells had an inactivating mutation
in the mDPM1 gene, indicating that mDPM1 is the
gene for class E mutant. In contrast, hDPM1 and
mDPM1 cDNA did not complement another Dol-P-Man synthesis mutant, hamster Lec15 cells, whereas yeast DPM1
restored both mutants. Therefore, in contrast to yeast, mammalian cells require hDPM1/mDPM1 protein and a product of another gene that is
defective in Lec15 mutant cells for synthesis of Dol-P-Man.
Department of Immunoregulation, Research
Institute for Microbial Diseases, Osaka University, Osaka and
§ Laboratory of Cell Engineering, National Institute of
Sericultural and Entomological Science, Tsukuba, Ibaraki, Japan
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