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PMID:14612445

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Citation

Koles, K, Irvine, KD and Panin, VM (2004) Functional characterization of Drosophila sialyltransferase. J. Biol. Chem. 279:4346-57

Abstract

Sialylation is an important carbohydrate modification of glycoconjugates in the deuterostome lineage of animals. By contrast, the evidence for sialylation in protostomes has been scarce and somewhat controversial. In the present study, we characterize a Drosophila sialyltransferase gene, thus providing experimental evidence for the presence of sialylation in protostomes. This gene encodes a functional alpha2-6-sialyltransferase (SiaT) that is closely related to the vertebrate ST6Gal sialyltransferase family, indicating an ancient evolutionary origin for this family. Characterization of recombinant, purified Drosophila SiaT revealed a novel acceptor specificity as it exhibits highest activity toward GalNAcbeta1-4GlcNAc carbohydrate structures at the non-reducing termini of oligosaccharides and glycoprotein glycans. Oligosaccharides are preferred over glycoproteins as acceptors, and no activity toward glycolipid acceptors was detected. Recombinant Drosophila SiaT expressed in cultured insect cells possesses in vivo and in vitro autosialylation activity toward beta-linked GalNAc termini of its own N-linked glycans, thus representing the first example of a sialylated insect glycoconjugate. In situ hybridization revealed that Drosophila SiaT is expressed during embryonic development in a tissue- and stage-specific fashion, with elevated expression in a subset of cells within the central nervous system. The identification of a SiaT in Drosophila provides a new evolutionary perspective for considering the diverse functions of sialylation and, through the powerful genetic tools available in this system, a means of elucidating functions for sialylation in protostomes.

Links

PubMed Online version:10.1074/jbc.M309912200

Keywords

Amino Acid Sequence; Animals; Cations, Divalent; Central Nervous System/embryology; Central Nervous System/enzymology; Drosophila melanogaster/embryology; Drosophila melanogaster/enzymology; Drosophila melanogaster/genetics; Evolution, Molecular; Gene Expression Regulation, Developmental; Genes, Insect; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Phylogeny; RNA, Messenger/genetics; RNA, Messenger/metabolism; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Sequence Homology, Amino Acid; Sialyltransferases/chemistry; Sialyltransferases/genetics; Sialyltransferases/metabolism; Substrate Specificity; Temperature

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

DROME:Q3YNC8

located_in

GO:0005576: extracellular region

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:Q3YNC8

involved_in

GO:0009311: oligosaccharide metabolic process

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

DROME:Q3YNC8

enables

GO:0008373: sialyltransferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

DROME:Q3YNC8

located_in

GO:0005794: Golgi apparatus

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:Q9GU23

located_in

GO:0005576: extracellular region

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:Q9GU23

located_in

GO:0005794: Golgi apparatus

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:Q9W121

located_in

GO:0005576: extracellular region

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:Q9W121

located_in

GO:0005794: Golgi apparatus

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:Q9W121

GO:0003835: beta-galactoside alpha-2,6-sialyltransferase activity

ECO:0000314:

F

Table 1 shows that the protein is specific to acceptors due to the activity.

complete
CACAO 10261

DROME:Q9W121

GO:0003835: beta-galactoside alpha-2,6-sialyltransferase activity

ECO:0000247:

UniProtKB:Q96JF0


F

Figure 7 shows that the function is an acceptor for oligosaccharides or glycoproteins.

complete
CACAO 10262

DROME:Q9W121

GO:0003835: beta-galactoside alpha-2,6-sialyltransferase activity

ECO:0000247:

UniProtKB:Q92182


F

Figure 7

complete
CACAO 10325

DROME:Q9W121

involved_in

GO:0009311: oligosaccharide metabolic process

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

DROME:Q9W121

part_of

GO:0005794: Golgi apparatus

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:Q9W121

part_of

GO:0005576: extracellular region

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:Q9W121

enables

GO:0008373: sialyltransferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

DROME:Q9W121

enables

GO:0003835: beta-galactoside alpha-2,6-sialyltransferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

DROME:Q9GU23

involved_in

GO:0009311: oligosaccharide metabolic process

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

DROME:Q9GU23

part_of

GO:0005576: extracellular region

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:Q9GU23

part_of

GO:0005794: Golgi apparatus

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:Q9GU23

enables

GO:0008373: sialyltransferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

Notes

See also

References

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