Glycobiology, Vol 9, 851-863, Copyright © 1999 by Oxford University Press
D Mercier, A Wierinckx, A Oulmouden, PF Gallet, MM Palcic, A Harduin-Lepers, P Delannoy, JM Petit, H Lev ziel and R Julien
In this study, we report the first isolation and characterization of a
bovine sialyltransferase gene. Bovine cDNAs prepared from different tissues
contain an open-reading frame encoding a 405 amino acid sequence showing
83%, 75%, and 60% identity with human, murine, and chicken ST6Gal I
(beta-galactoside alpha2,6-sialyltransferase) sequences, respectively.
Whentransfected into COS-7 cells, a recombinant enzyme wasobtained which
catalyzed the in vitro alpha2, 6- sialylation of LacNAc
(NeuAcalpha2-6Galbeta1-4GlcNAc) and LacdiNAc
(NeuAcalpha2-6GalNAcbeta1-4GlcNAc) acceptor substrates. The K (m) values
were 2.8 and 6.9 mM, respectively. Different relative efficiencies (V (max)
/K (m) ) for the two precursors (36 for LacNAc and 4.3 for LacdiNAc) were
observed. Bovine ST6Gal I gene consists of four 5'-untranslated exons E(-2)
to E(1), and five coding exons from E(2) to E(6). This later carries a
3'-untranslated region of 2. 7 kb. Gene sequence spans at least 80 kb of
genomic DNA. Two processed pseudogenes have been identified. They are 94.3
and 95.6% similar to the bovine cDNA, respectively. Three families of mRNA
isoforms were isolated. They differed by their 5'-untranslated regions and
could be generated by three tissue-specific promoters. Family 1 is made up
of exons E(-2) and E(1) to E(6), family 2 of exons E(-1) to E(6), and
family 3 of exons E(1) to E(6). Tissular distribution of transcript
families appears noticeably different than those described in human and
rat.
Molecular cloning, expression and exon/intron organization of the bovine beta-galactoside alpha2,6-sialyltransferase gene [In Process Citation]
Institut de Biotechnologie, Faculte des Sciences, Universite de Limoges, 87060 Limoges, France, Department of Chemistry, University of Alberta, Edmonton, Alberta T6G 2G2, Canada, Laboratoire de Chimie Biologique, UMR no. 8576 du CNRS, Universite.
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