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  • The evolution of galactose α2,3-sialyltransferase: Ciona intestinalis ST3GAL I/II and Takifugu rubripes ST3GAL II sialylate Galβ1,3GalNAc structures on glycoproteins but not glycolipids

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    Author(s)
    Lehmann, Friederike
    Kelm, Sorge
    Dietz, Frank
    von Itzstein, Mark
    Tiralongo, Joe
    Griffith University Author(s)
    von Itzstein, Mark
    Tiralongo, Joe
    Lehmann, Friederike
    Year published
    2008
    Metadata
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    Abstract
    Sialyltransferases are a family of enzymes catalyzing the transfer of sialic acid residues to terminal non-reducing positions of oligosaccharide chains of glycoproteins and glycolipids. Although expression of sialic acid is well documented in animals of the deuterostomian lineage, sialyltransferases have been predominantly described for relatively recent vertebrate lineages such as birds and mammals. This study outlines the characterization of the only sialyltransferase gene found in the tunicate Ciona intestinalis, the first such report of a non-vertebrate deuterostomian sialyltransferase, which has been discussed as a ...
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    Sialyltransferases are a family of enzymes catalyzing the transfer of sialic acid residues to terminal non-reducing positions of oligosaccharide chains of glycoproteins and glycolipids. Although expression of sialic acid is well documented in animals of the deuterostomian lineage, sialyltransferases have been predominantly described for relatively recent vertebrate lineages such as birds and mammals. This study outlines the characterization of the only sialyltransferase gene found in the tunicate Ciona intestinalis, the first such report of a non-vertebrate deuterostomian sialyltransferase, which has been discussed as a possible orthologue of the common ancestor of galactose a2,3-sialyltransferases. We also report for the first time the characterization of a ST3Gal II gene from the bony fish Takifugu rubripes. We demonstrate that both genes encode functional a2,3-sialyltransferases that are structurally and functionally related to the ST3Gal family of mammalian sialyltransferases. However, characterization of the recombinant, purified forms of both enzymes reveal novel acceptor substrate specificities, with sialylation of the disaccharide Gal߱-3GalNAc and asialofetuin, but not GM1 or GD1b observed. This is in contrast to the mammalian ST3Gal II that predominantly sialylates gangliosides. Taken together the ceramide binding/recognition site previously proposed for the mouse ST3Gal II might represent a unique feature of mammalian ST3Gal II that is missing in the evolutionary more distant fish and tunicate species reported here. This suggests that during the evolution of the ST3Gal II, probably following the separation of the teleosts, a significant shift in substrate specificity enabling the sialylation of gangliosides took place.
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    Journal Title
    Glycoconjugate Journal
    Volume
    25
    Issue
    4
    DOI
    https://doi.org/10.1007/s10719-007-9078-4
    Copyright Statement
    © 2008 Springer Netherlands. This is an electronic version of an article published in Glycoconjugate Journal, Vol. 25(4), 2008, pp. 323-334. Glycoconjugate Journal is available online at: http://link.springer.com// with the open URL of your article.
    Subject
    Biochemistry and cell biology
    Enzymes
    Medical microbiology
    Neurosciences
    Publication URI
    http://hdl.handle.net/10072/23612
    Collection
    • Journal articles

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