+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Transcriptional regulation of the human UDP-GlcNAc:alpha-6-D-mannoside beta-1-2-N-acetylglucosaminyltransferase II gene (MGAT2) which controls complex N-glycan synthesis



Transcriptional regulation of the human UDP-GlcNAc:alpha-6-D-mannoside beta-1-2-N-acetylglucosaminyltransferase II gene (MGAT2) which controls complex N-glycan synthesis



Glycoconjugate Journal 15(3): 301-308



UDP-GlcNAc:alpha-6-D-mannoside beta-1,2-N-acetylglucosaminyltransferase II (GnT II; EC 2.4.1.143) is essential for the normal assembly of complex Asn-linked glycans. Northern analysis showed a major transcript at 2.0 kb and a minor band at approximately 2.9 kb in five different human cell lines. The gene (MGAT2) has three AATAAA polyadenylation sites at 68, 688 and 846 bp downstream of the translation stop codon. 3'-RACE (rapid amplification of cDNA ends) using RNA from the human cell line LS-180 indicated that all three sites were utilized for transcription termination. 5'-RACE and RNase protection analyses showed multiple transcription initiation sites at -440 to -489 bp relative to the ATG translation start codon (+1). The data show that the entire GnT II gene is on a single exon. The gene has a CCAAT box at -587 bp but lacks a TATA box and the 5'-untranslated region is GC-rich and contains consensus sequences suggestive of multiple binding sites for Sp1; these properties are typical for housekeeping genes. A series of chimeric constructs containing different lengths of the 5'-untranslated region fused to the chloramphenicol acetyltransferase (CAT) reporter gene were tested in transient transfection experiments using HeLa cells. The CAT activity of the construct containing the longest insert (-1076 bp relative to the ATG start codon) showed a approximately 38-fold increase as compared to that of the control. Removal of the region between -636 and -553 bp caused a dramatic decrease in CAT activity indicating this to be the main promoter region of the gene.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 047813647

Download citation: RISBibTeXText

PMID: 9579808


Related references

The human UDP-N-acetylglucosamine: alpha-6-D-mannoside-beta-1,2- N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein. European Journal of Biochemistry 231(2): 317-328, 1995

Organization of the human beta-1,2-N-acetylglucosaminyltransferase I gene (MGAT1), which controls complex and hybrid N-glycan synthesis. Biochemical Journal 321: 465-474, 1997

Control of glycoprotein synthesis. IX. A terminal Man alpha l-3Man beta 1- sequence in the substrate is the minimum requirement for UDP-N-acetyl-D-glucosamine: alpha-D-mannoside (GlcNAc to Man alpha 1-3) beta 2-N-acetylglucosaminyltransferase I. Canadian Journal of Biochemistry and Cell Biology 62(6): 409-417, 1984

Cloning and expression of a novel UDP-GlcNAc:alpha-D-mannoside beta1,2-N-acetylglucosaminyltransferase homologous to UDP-GlcNAc:alpha-3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I. Biochemical Journal 361(Pt 1): 153-162, 2002

Organization of the human β-1,2-N-acetylglucosaminyltransferase I gene (MGAT1), which controls complex and hybrid N-glycan synthesis. Biochemical Journal 321(2): 465-474, 1997

Purification of rat kidney udp n acetylglucosamine alpha mannoside beta 1 6n acetylglucosaminyltransferase glcnac tv. Journal of Cell Biology 111(5 Part 2): 199A, 1990

Mice with a homozygous deletion of the Mgat2 gene encoding UDP-N-acetylglucosamine:alpha-6-D-mannoside beta1,2-N-acetylglucosaminyltransferase II: a model for congenital disorder of glycosylation type IIa. Biochimica et Biophysica Acta 1573(3): 301-311, 2002

Cloning and expression of a novel UDP-GlcNAc:α-d-mannoside β1,2-N-acetylglucosaminyltransferase homologous to UDP-GlcNAc:α-3-d-mannoside β1,2-N-acetylglucosaminyltransferase I. Biochemical Journal 361(1): 153-162, 2002

Increased UDP-GlcNAc: alpha-mannoside beta(1----4) N-acetylglucosaminyltransferase activity during chick embryo development. Biochimica et Biophysica Acta 1054(2): 149-153, 1990

The role of the GlcNAcbeta1,2Manalpha- moiety in mammalian development. Null mutations of the genes encoding UDP-N-acetylglucosamine: alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I and UDP-N-acetylglucosamine: alpha-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I.2 cause embryonic lethality and congenital muscular dystrophy in mice and men, respectively. Biochimica et Biophysica Acta 1573(3): 292-300, 19 December, 2002

Regulation of expression of the human beta-1,2-N-acetylglucosaminyltransferase II gene (MGAT2) by Ets transcription factors. Biochemical Journal 347(Pt 2): 511-518, 2000

The expression of IV6 beta[Gal beta 1-4(Fuc alpha 1-3)GlcNAc]-Gb5Cer in mouse kidney is controlled by the Gsl-5 gene through regulation of UDP-GlcNAc:Gb5Cer beta 1-6N-acetylglucosaminyltransferase activity. Journal of Biochemistry 108(1): 103-108, 1990

Increased UDP-GlcNAc: alpha-mannoside beta(1 linked to 4) N-acetylglucosaminyltransferase activity during chick embryo development. Biochimica et biophysica acta: International journal of biochemistry and biophysics, 1054(2): 149-153, 1990

Removal of 106 amino acids from the N-terminus of UDP-GlcNac: alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I does not inactivate the enzyme. Glycoconjugate Journal 15(2): 193-197, 1998

Activity of UDP-GlcNAc:alpha-mannoside beta(1,6)N-acetylglucosaminyltransferase (GnT V) in cultured cells using a synthetic trisaccharide acceptor. Biochemical and Biophysical Research Communications 146(2): 679-684, 1987