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J. Biol. Chem., Vol. 277, Issue 25, 22829-22838, June 21, 2002
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From the UDP-N-acetylglucosamine: The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF154122 (gly-2), AY037800 (cm20c4), and AY037802 (yk126h8). Appropriate data have also been contributed to ACeDB.
The Caenorhabditis elegans Gene,
gly-2, Can Rescue the
N-Acetylglucosaminyltransferase V Mutation of Lec4
Cells*
,,§¶,§, and§
Samuel Lunenfeld Research Institute, Mount
Sinai Hospital, Toronto, Ontario M5G 1X5 and § Department
of Molecular and Medical Genetics, University of Toronto, Toronto,
Ontario, M55 1A8, Canada
-6-D-mannoside
-1,6-N-acetylglucosaminyltransferase V (GlcNAc-TV) is a
regulator of polylactosamine-containing N-glycans and is
causally involved in T cell regulation and tumor metastasis. The
Caenorhabditis elegans genome contains a single orthologous
gene, gly-2, that is transcribed and encodes a 669-residue type II membrane protein that is 36.7% identical to mammalian GlcNAc-TV (Mgat-5). Recombinant GLY-2 possessed GlcNAc-TV
activity when assayed in vitro, and protein truncations
demonstrated that the N-terminal boundary of the catalytic domain is
Ile-138. gly-2 complemented the Phaseolus
vulgaris leucoagglutinin binding defect of Chinese hamster ovary
Lec4 cells, whereas GLY-2(L116R), an equivalent mutation to that
which causes the Lec4A phenotype, could not. We conclude that
the worm gene is functionally interchangeable with the mammalian form.
GlcNAc-TV activity was detected in wild-type animals but not those
homozygous for a deletion allele of gly-2. Activity was
restored in mutant animals by an extrachromosomal array that
encompassed the gly-2 gene. Green fluorescent
protein reporter transgenes driven by the gly-2 promoter
were expressed by developing embryos from the late comma stage onward,
present in a complex subset of neurons in larvae and, in addition, the spermathecal and pharyngeal-intestinal valves and certain vulval cells
of adults. However, no overt phenotypes were observed in animals
homozygous for deletion alleles of gly-2.
*
This work was funded by a grant from the National Cancer
Institute of Canada.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Samuel Lunenfeld
Research Inst., Mount Sinai Hospital, 600 University Ave., Toronto, Ontario M5G 1X5, Canada. Tel.: 416-586-8233; Fax: 416-586-8857; E-mail:
dennis@mshri.on.ca.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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