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(Received for publication, November 30, 1995) A cDNA encoding a novel sialyltransferase has been isolated
employing the polymerase chain reaction using degenerate primers to
conserved regions of the sialylmotif that is present in all eukaryotic
members of the sialyltransferase gene family examined to date. The cDNA
sequence revealed an open reading frame coding for 305 amino acids,
making it the shortest sialyltransferase cloned to date. This open
reading frame predicts all the characteristic structural features of
other sialyltransferases including a type II membrane protein topology
and both sialylmotifs, one centrally located and the second in the
carboxyl-terminal portion of the cDNA. When compared with all other
sialyltransferase cDNAs, the predicted amino acid sequence displays the
lowest homology in the sialyltransferase gene family. Northern analysis
shows this sialyltransferase to be developmentally regulated in brain
with expression persisting through adulthood in spleen, kidney, and
lung. Stable transfection of the full-length cDNA in the human kidney
carcinoma cel line 293 produced an active sialyltransferase with marked
specificity for the sialoside, Neu5Ac
Volume 271,
Number 13,
Issue of March 29, 1996 pp. 7450-7459
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
2,6-Sialyltransferase Specific for Sialylated Glycoconjugates
2,3Gal
1,3GalNAc and
glycoconjugates carrying the same sequence such as G and
fetuin. The disialylated tetrasaccharide formed by reacting the
sialyltransferase with the aforementioned sialoside was analyzed by
one- and two-dimensional
H and C NMR
spectroscopy and was shown to be the
Neu5Ac
2,3Gal1,3(Neu5Ac2,6)GalNAc sialoside. This
indicates that the enzyme is a GalNAc 2,6-sialyltransferase. Since
two other ST6GalNAc sialyltransferase cDNAs have been isolated, this
sialyltransferase has been designated ST6GalNAc III. Of these three,
ST6GalNAc III displays the most restricted acceptor specificity and is
the only sialyltransferase cloned to date capable of forming the
developmentally regulated ganglioside G from
G
.
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