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Papers In Press, published online ahead of print April 5, 2002
Samuel Lunenfeld Research Institute, Room 988, Mount Sinai Hospital, Toronto, ON M5G 1X5
Corresponding Author: dennis{at}mshri.on.ca
UDP-N-acetylglucosamine:(alpha)-3-D-mannoside (beta)-1,6-N-acetylglucosaminyltransferase V (GlcNAc-TV) is a regulator of polylactosamine containing N-glycans, and causally involved in T cell regulation and tumour metastasis. The C. 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 I138. gly-2 complemented the L-PHA-binding defect of Chinese hamster ovary Lec4 cells, whereas GLY-2(L116R), an equivalent mutation to that which causes the Lec4A phenotype, could not rescue. 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 extrachomosomal array that encompassed the gly-2 gene. GFP 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 addtion, 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.
J. Biol. Chem, 10.1074/jbc.M201390200
Submitted on February 11, 2002
Revised on March 28, 2002
Accepted on April 4, 2002
The C. elegans gene, gly-2, can rescue the N-acetylglucosaminyltransferase V mutation of Lec4 cells
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