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Glycobiology Advance Access published online on May 28, 2003
Glycobiology, doi:10.1093/glycob/cwg080
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Submitted on February 21, 2003
Revised on May 7, 2003
Accepted on May 15, 2003

© 2003 Oxford University Press

ORIGINAL ARTICLES

Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase

Adrian R. Walmsley 1 Nigel M. Hooper 1*

1 School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, UK

* To whom correspondence should be addressed. E-mail: n.m.hooper{at}leeds.ac.uk.

Abstract

In vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley & Hooper, 2003, Biochemical Journal 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosyl-phosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilisation of sequons in some proteins is independent of their distance from the C-terminus.


N-glycosylation, oligosaccharyltransferase, prion protein, membrane dipeptidase, glycosyl-phosphatidylinositol anchor
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