Marine invertebrate sialyltransferase of the sea squirt Ciona savignyi sialylated core 1 O-linked glycans

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Marine invertebrate sialyltransferase of the sea squirt Ciona savignyi sialylated core 1 O-linked glycans
Seonghun KimJinhyuk LeeDoo-Byoung OhOhsuk Kwon
Bibliographic Citation
International Journal of Biological Macromolecules, vol. 194, pp. 366-376
Publication Year
An invertebrate sialyltransferase, cST3Gal-I, identified from the sea squirt Ciona savignyi, was functionally characterized in vitro using recombinant enzyme expressed in yeast strains. cST3Gal-I was localized to the Golgi membrane when expressed in Saccharomyces cerevisiae. Enzymatic characterization for substrate specificity and kinetic property indicate that cST3Gal-I prefers O-glycans, rather than N-glycan, of asialoglycoproteins as substrates. Interestingly, C. savignyi sialyltransferase exhibited effectively Neu5Ac transfer to core 1 O-glycan, Gal β(1,3)GalNAc, compared to orthologous human glycosyltransferase. Further, it is shown that cST3Gal-I catalyzes the formation of α(2,3)-linkage, through lectin blot analysis with Maackia amurensis lectin and by linkage-specific sialidase treatments. The putative active sites of cST3Gal-I for putative acid/base catalysts and sialic acid acceptor/donor substrate bindings were also identical to the counterpart residues of a mammalian enzyme, porcine ST3Gal-I, as predicted through homologous structure modeling. These results could imply that an ancestral tunicate ST3Gal-I in C. savignyi would prefer O-glycan onto glycoproteins as its sialic acid acceptor than vertebrate enzymes.
SialyltransferaseCiona savignyiSialic acidα(2,3)-linkageMarine invertebrateSialyl O-glycan
Appears in Collections:
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Aging Convergence Research Center > 1. Journal Articles
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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