The influence of flanking sequences on O-glycosylation

Brian O'Connell, Lawrence A. Tabak, Narayanan Ramasubbu

Research output: Contribution to journalArticlepeer-review

77 Scopus citations

Abstract

The influence of flanking sequences on O-glycosylation of serine and threonine residues was explored by comparison of known acceptor sites. Positions -6, -1 and +3 relative to the site were identified as particularly significant. To test the hypothesis that O-glycosylation could be affected by amino acid sequence, a series of test peptides was made containing substitutions at the sensitive positions. In vitro glycosylation of the peptides confirmed that the acceptor status of threonine was markedly influenced by the residues present at positions -6, -1 and +3. Circular dichroism indicated that peptides which had random structure were glycosylated, except when they contained a charged residue at position -1.

Original languageEnglish (US)
Pages (from-to)1024-1030
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume180
Issue number2
DOIs
StatePublished - Oct 31 1991
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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