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A more recent version of this article appeared on May 5, 2006
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Papers In Press, published online ahead of print March 7, 2006
J. Biol. Chem, 10.1074/jbc.M512769200
Submitted on November 29, 2005
Revised on February 14, 2006
Accepted on March 7, 2006

Null mutations in Drosophila N-acetylglucosaminyltransferase I produce defects in locomotion and a reduced lifespan

Mohan Sarkar, Peter A. Leventis, Cristina I. Silvescu, Vernon N. Reinhold, Harry Schachter, and Gabrielle L. Boulianne

Program in Structural Biology & Biochemistry, The Hospital for Sick Children, Toronto, Ontario M5G 1X8

Corresponding Author: harry{at}sickkids.ca

UDP-GlcNAc:a3-D-mannoside ß1,2-N-acetylglucosaminyltransferase I (GnTI, encoded by Mgat1) controls the synthesis of hybrid, complex and paucimannose N-glycans. Mice make hybrid and complex but little or no paucimannose N-glycans. In contrast, Drosophila melanogaster and Caenorhabditis elegans make paucimannose but little or no hybrid nor complex N-glycans. To determine the functional requirement for GnTI in Drosophila, we generated null mutations by imprecise excision of a nearby transposable element. Extracts from homozygous Mgat1 null mutants showed no GnTI enzyme activity. Moreover, mass spectrometric analysis of these extracts showed dramatic changes in N-glycans compatible with lack of GnTI enzyme activity. Interestingly, Mgat1 null mutants are homozygous viable but exhibit pronounced defects in locomotory activity when compared to Mgat1 heterozygotes or wildtype flies. In addition, null mutants are male sterile and have a severely reduced mean and maximum lifespan. Microscopic examination of mutant adult fly brains showed the presence of fused ß lobes. The removal of both maternal and zygotic Mgat1 also gave rise to embryos that no longer express the horseradish peroxidase (HRP) antigen within the central nervous system. Taken together, the data indicate that GnTI-dependent N-glycans are required for locomotory activity, lifespan and brain development in Drosophila.


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