title: Murine hepatic beta-galactoside alpha 2,6-sialyltransferase gene expression involves usage of a novel upstream exon region.
abstract: ST6Gal I (beta-galactoside alpha 2,6-sialyltransferase, SiaT-1, ST6N, EC 2.4.99.1) mediates the attachment of the alpha 2,6-sialyl linkage common on N-linked glycans. Previous work suggests substantial inter-species conservation in SIAT1, the gene encoding ST6Gal I. In human and in rat, hepatic-specific SIAT1 transcription is initiated at Exon I. Here we report a surprising departure in the structural organization of the murine ST6Gal I gene. By a combination of primer extension analysis, 5'-RACE analysis, and analysis of genomic sequences, we show that the murine hepatic ST6Gal I mRNA contains a novel region 5' of Exon I. This novel sequence is encoded on a discrete upstream exon, Exon H. In contrast to human and rat hepatic ST6Gal I, the murine mRNA is transcriptionally initiated at the start of Exon H. Differential mRNA blot analysis indicates that transcripts containing Exon H sequences are preferentially expressed in liver.
authors.affiliation: Department of Molecular and Cellular Biology, Roswell Park Cancer Institute, Buffalo, NY 14263, USA.
authors.forename: Y P
authors.initials: YP
authors.lastname: Hu
authors.forename: M
authors.initials: M
authors.lastname: Dalziel
authors.forename: J T
authors.initials: JT
authors.lastname: Lau
mesh_terms: D000818:Animals; D001483:Base Sequence; D017931:DNA Primers; D005091:Exons; D015971:Gene Expression Regulation, Enzymologic; D015698:Genomic Library; D006801:Humans; D008099:Liver / Q000201:enzymology*; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D008969:Molecular Sequence Data; D009928:Organ Specificity; D016133:Polymerase Chain Reaction; D051381:Rats; D015183:Restriction Mapping; D012799:Sialyltransferases / Q000096:biosynthesis* / Q000235:genetics; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
chemical_list: D017931:DNA Primers; D012799:Sialyltransferases; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase