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J Biol Chem, Vol. 274, Issue 1, 288-297, January 1, 1999
§,,,§
From the UDP-N-acetylglucosamine: Department of Structural Biology and
Biochemistry, The Hospital for Sick Children, Toronto, Ontario M5G 1X8,
Canada, the § Department of Biochemistry, University of
Toronto, Toronto, Ontario M5S 1A8 Canada, and the ¶ Department of
Molecular and Medical Genetics, University of Toronto,
Toronto, Ontario M5S 1A8, Canada
-3-D-mannoside
-1,2-N-acetylglucosaminyltransferase I (GnT I) is
a key enzyme in the synthesis of Asn-linked complex and hybrid glycans.
Studies on mice with a null mutation in the GnT I gene have indicated
that N-glycans play critical roles in mammalian
morphogenesis. This paper presents studies on N-glycans
during the development of the nematode Caenorhabditis elegans. We have cloned cDNAs for three predicted C. elegans genes homologous to mammalian GnT I (designated
gly-12, gly-13, and gly-14). All
three cDNAs encode proteins (467, 449, and 437 amino acids,
respectively) with the domain structure typical of previously cloned
Golgi-type glycosyltransferases. Expression in both insect cells and
transgenic worms showed that gly-12 and gly-14,
but not gly-13, encode active GnT I. All three genes were
expressed throughout worm development (embryo, larval stages L1-L4,
and adult worms). The gly-12 and gly-13
promoters were expressed from embryogenesis to adulthood in many
tissues. The gly-14 promoter was expressed only in gut
cells from L1 to adult developmental stages. Transgenic worms that
overexpress any one of the three genes show no obvious phenotypic
defects. The data indicate that C. elegans is a suitable
model for further study of the role of complex N-glycans in development.
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