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Originally published In Press as doi:10.1074/jbc.M202684200 on March 29, 2002

J. Biol. Chem., Vol. 277, Issue 25, 22623-22638, June 21, 2002
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Functional Conservation of Subfamilies of Putative UDP-N-acetylgalactosamine:Polypeptide N-Acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and Mammals
ONE SUBFAMILY COMPOSED OF l(2)35Aa IS ESSENTIAL IN DROSOPHILA*

Tilo Schwientekabc, Eric P. Bennettacd, Carlos Florese, John Thackerf, Martin Hollmanng, Celso A. Reish, Jane Behrensa, Ulla Mandela, Birgit Kecka, Mireille A. Schäferg, Kim Haselmanni, Roman Zubarevi, Peter Roepstorffi, Joy M. Burchellj, Joyce Taylor-Papadimitriouj, Michael A. Hollingsworthk, and Henrik Clausenal

From the a School of Dentistry, University of Copenhagen, Nørre Alle 20, 2200 Copenhagen N, Denmark, e University of Wisconsin, Laboratory of Genetics, Madison, Wisconsin 53706, f Medical Research Council, Radiation and Genome Stability Unit, Oxfordshire OX11 0RD, United Kingdom, g Zoologisches Institut-Entwicklungsbiologie, Abt. Molekulare Entwicklungsgenetik, Georg-August-Universität Göttingen, Humboldtallee 34A, 37073 Göttingen, Germany, h Institute of Molecular Pathology and Immunology of the University of Porto, IPATIMUP, 4200 Porto, Portugal, the i Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense University, Odense 5230, Denmark, j Imperial Cancer Research Fund, Breast Cancer Biology Group, 3rd Floor, Thomas Guy House, Guy's Hospital, London SE1 9RT, United Kingdom, and the k Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198

The completed fruit fly genome was found to contain up to 15 putative UDP-N-acetyl-alpha -D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) genes. Phylogenetic analysis of the putative catalytic domains of the large GalNAc-transferase enzyme families of Drosophila melanogaster (13 available), Caenorhabditis elegans (9 genes), and mammals (12 genes) indicated that distinct subfamilies of orthologous genes are conserved in each species. In support of this hypothesis, we provide evidence that distinctive functional properties of Drosophila and human GalNAc-transferase isoforms were exhibited by evolutionarily conserved members of two subfamilies (dGalNAc-T1 (l(2)35Aa) and GalNAc-T11; dGalNAc-T2 (CG6394) and GalNAc-T7). dGalNAc-T1 and novel human GalNAc-T11 were shown to encode functional GalNAc-transferases with the same polypeptide acceptor substrate specificity, and dGalNAc-T2 was shown to encode a GalNAc-transferase with similar GalNAc glycopeptide substrate specificity as GalNAc-T7. Previous data suggested that the putative GalNAc-transferase encoded by l(2)35Aa had a lethal phenotype (Flores, C., and Engels, W. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 2964-2969), and this was substantiated by sequencing of three lethal alleles l(2)35AaHG8, l(2)35AaSF12, and l(2)35AaSF32. The finding that subfamilies of GalNAc-transferases with distinct catalytic functions are evolutionarily conserved stresses that GalNAc-transferase isoforms may serve unique biological functions rather than providing functional redundancy, and this is further supported by the lethal phenotype of l(2)35Aa.

* This work was supported by the Danish Cancer Society, the Velux Foundation, the Danish Research Councils, the EU Biotech 5th Framework, National Institutes of Health Grants 1 RO1 CA66234 and GM30948, and FCT-POCTI/36376/99.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.

Partial data were presented in abstract form at the XVI International Symposium on Glycoconjugates (49, 50).

b To whom correspondence may be addressed: Institut für Biochemie II, Medizinische Fakultät der Universität Köln; Joseph-Stelzmann-Strasse 52, 50931 Köln, Germany. E-mail: akd88@uni-koeln.de.

c These authors contributed equally to this work.

d To whom correspondence may be addressed: School of Dentistry, Nørre Alle 20, DK-2200 Copenhagen N, Denmark. Tel.: 45-35326835; Fax: 45-35326505; E-mail: epb@odont.ku.dk.

l To whom correspondence may be addressed: School of Dentistry, Nørre Alle 20, DK-2200 Copenhagen N, Denmark. Tel.: 45-35326835; Fax: 45-35326505; E-mail: hc@odont.ku.dk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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