Functional expression and genomic structure of human N-acetylglucosamine-6-O-sulfotransferase that transfers sulfate to beta-N-acetylglucosamine at the nonreducing end of an N-acetyllactosamine sequence

Biochim Biophys Acta. 2000 Oct 18;1523(2-3):269-76. doi: 10.1016/s0304-4165(00)00136-7.

Abstract

The cDNA and gene encoding human N-acetylglucosamine-6-O-sulfotransferase (Gn6ST) have been cloned. Comparative analysis of this cDNA with the mouse Gn6ST sequence indicates 96% amino acid identity between the two sequences. The expression of a soluble recombinant form of the protein in COS-1 cells produced an active sulfotransferase, which transferred sulfate to the terminal GlcNAc in GlcNAcbeta1-O-CH(3), GlcNAcbeta1-3Galbeta1-O-CH(3) and GlcNAcbeta1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Gl cNAc but not in GlcNAcalpha1-4GlcAbeta1-3Galbeta1-3Galbeta1-4 Xylbeta1-O-Ser. In addition, neither Galbeta1-4GlcNAcbeta1-O-naphthalenemethanol nor GalNAcbeta1-4GlcAbeta1-3Galbeta1-3Galbeta1-4X ylbeta1-O-Ser were utilized as acceptors. These findings indicate that a terminal beta-linked GlcNAc residue is necessary for acceptor substrates of Gn6ST. The human Gn6ST gene spans about 7 kb, consists of two exons and exhibits an intron-less coding region.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / metabolism
  • Amino Acid Sequence
  • Amino Sugars / metabolism
  • Animals
  • Base Sequence
  • COS Cells
  • Carbohydrate Sulfotransferases
  • Chlorocebus aethiops
  • Humans
  • Mice
  • Molecular Sequence Data
  • Recombinant Proteins / metabolism
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Sequence Homology, Nucleic Acid
  • Substrate Specificity
  • Sulfotransferases / chemistry
  • Sulfotransferases / genetics*
  • Sulfotransferases / metabolism*
  • Transfection

Substances

  • Amino Sugars
  • Recombinant Proteins
  • N-acetyllactosamine
  • Sulfotransferases
  • Acetylglucosamine

Associated data

  • GENBANK/AB021124
  • GENBANK/AB021125