PUBLICATION
Molecular cloning of pigeon UDP-galactose:{beta}-D-galactoside {alpha}1,4-galactosyltransferase and UDP-galactose:{beta}-D-galactoside {beta}1,4-galactosyltransferase, two novel enzymes catalyzing the formation of Gal{alpha}1-4Gal{beta}1-4Gal{beta}1-4GlcNAc sequence
- Authors
- Suzuki, N., and Yamamoto, K.
- ID
- ZDB-PUB-091215-40
- Date
- 2010
- Source
- The Journal of biological chemistry 285(8): 5178-5187 (Journal)
- Registered Authors
- Keywords
- GLYCOPROTEINS, Carbohydrate biosynthesis, Carbohydrate structure, Enzyme structure, Enzymes, Gb3 synthase, P1 antigen, glycan diversity, glycosyltransferase, molecular evolution
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Catalysis
- Chickens/genetics
- Chickens/metabolism
- Cloning, Molecular/methods
- Columbidae/genetics*
- Columbidae/metabolism
- Evolution, Molecular
- Galactosyltransferases/genetics*
- Galactosyltransferases/metabolism
- Glycosylation
- Humans
- Immunoglobulin G/genetics
- Immunoglobulin G/metabolism
- Molecular Sequence Data
- Sequence Homology, Amino Acid
- Species Specificity
- PubMed
- 19959475 Full text @ J. Biol. Chem.
Citation
Suzuki, N., and Yamamoto, K. (2010) Molecular cloning of pigeon UDP-galactose:{beta}-D-galactoside {alpha}1,4-galactosyltransferase and UDP-galactose:{beta}-D-galactoside {beta}1,4-galactosyltransferase, two novel enzymes catalyzing the formation of Gal{alpha}1-4Gal{beta}1-4Gal{beta}1-4GlcNAc sequence. The Journal of biological chemistry. 285(8):5178-5187.
Abstract
We previously found that pigeon IgG possesses unique N-glycan structures that contain the Galalpha1-4Galbeta1-4Galbeta1-4GlcNAc sequence at their non-reducing termini. This sequence is most likely produced by putative alpha1,4- and beta1,4-galactosyltransferases (GalTs), which are responsible for the biosynthesis of the Galalpha1-4Gal and Galbeta1-4Gal sequences on the N-glycans, respectively. Since no such glycan structures have been found in mammalian glycoproteins, the biosynthetic enzymes that produce these glycans are likely to have distinct substrate specificities from the known mammalian GalTs. To study these enzymes, we cloned the pigeon liver cDNAs encoding alpha4GalT and beta4GalT by expression cloning, and characterized these enzymes using the recombinant proteins. The deduced amino acid sequence of pigeon alpha4GalT has 58.2% identity to human alpha4GalT, and 68.0% and 66.6% identity to putative alpha4GalTs from chicken and zebra finch, respectively. Unlike human and putative chicken alpha4GalTs, which possess globotriosylceramide (Gb3) synthase activity, pigeon alpha4GalT preferred to catalyze formation of Galalpha1-4Gal sequence on glycoproteins. In contrast, the sequence of pigeon beta4GalT revealed a type II transmembrane protein consisting of 438 amino acid residues, with no significant homology to the glycosyltransferases so far identified from mammals and chicken. However, hypothetical proteins from zebra finch (78.8% identity), frogs (58.9--60.4%), zebrafish (37.1--43.0%), and spotted green pufferfish (43.3%) were similar to pigeon beta4GalT, suggesting that the pigeon beta4GalT gene was inherited from the common ancestors of these vertebrates. The sequence analysis revealed that pigeon beta4GalT and its homologs form a new family of glycosyltransferases.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping