A necessary and sufficient determinant for protein-selective glycosylation in vivo

Erin Miller, Dorothy Fiete, Nicquet M.J. Blake, Mary Beranek, Edward L. Oates, Yiling Mi, Daniel S. Roseman, Jacques U. Baenziger

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


A limited number of glycoproteins including luteinizing hormone and carbonic anhydrase-VI (CA6) bear N-linked oligosaccharides that are modified with β1,4-linked N-acetylgalactosamine (GalNAc). The selective addition of GalNAc to these glycoproteins requires that the β1,4-N- acetylgalactosaminyl-transferase (βGT) recognize both the oligosaccharide acceptor and a peptide recognition determinant on the substrate glycoprotein. We report here that two recently cloned βGTs, βGT3 and βGT4, that are able to transfer GalNAc to GlcNAc in β1,4-linkage display the necessary glycoprotein specificity in vivo. Both βGTs transfer GalNAc to N-linked oligosaccharides on the luteinizing hormone α subunit and CA6 but not to those on transferrin (Trf). A single peptide recognition determinant encoded in the carboxyl-terminal 19-amino acid sequence of bovine CA6 mediates transfer of GalNAc to each of its two N-linked oligosaccharides. The addition of this 19-amino acid sequence to the carboxyl terminus of Trf confers full acceptor activity onto Trf for both βGT3 and βGT4 in vivo. The complete 19-amino acid sequence is required for optimal GalNAc addition in vivo, indicating that the peptide sequence is both necessary and sufficient for recognition by βGT3 and βGT4.

Original languageEnglish
Pages (from-to)1985-1991
Number of pages7
JournalJournal of Biological Chemistry
Issue number4
StatePublished - Jan 25 2008


Dive into the research topics of 'A necessary and sufficient determinant for protein-selective glycosylation in vivo'. Together they form a unique fingerprint.

Cite this