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Papers In Press, published online ahead of print March 29, 2002
J. Biol. Chem, 10.1074/jbc.M202684200
Submitted on March 20, 2002
Revised on March 28, 2002
Accepted on March 29, 2002

Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine: Polypeptide N-acetylgalactosaminyltransferases in drosophila, C. elegans and mammals: One subfamily comprised of l(2)35Aa is essential in drosophila

Tilo J. Schwientek, Eric P. Bennett, Carlos Flores, John Thacker, Martin Hollman, Celso A. Reis, Jane Behrens, Ulla Mandel, Birgit Keck, Mireille A. Schafer, Kim Hazelmann, Roman Zubarev, Peter Roepstorff, Michael A. Hollingsworth, and Henrik Clausen

School of Dentistry, Copenhagen University, Copenhagen N DK-2200

Corresponding Author: hc{at}odont.ku.dk

The completed fruit fly genome was found to contain up to 15 putative 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 evolutionary 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.


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