TY - JOUR
T1 - The influence of flanking sequences on O-glycosylation
AU - O'Connell, Brian
AU - Tabak, Lawrence A.
AU - Ramasubbu, Narayanan
N1 - Funding Information:
Acknowledgments: This work was supported in part by National Institutes of Health Grants DE-
PY - 1991/10/31
Y1 - 1991/10/31
N2 - 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.
AB - 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.
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U2 - 10.1016/S0006-291X(05)81168-4
DO - 10.1016/S0006-291X(05)81168-4
M3 - Article
C2 - 1953707
AN - SCOPUS:0025746320
SN - 0006-291X
VL - 180
SP - 1024
EP - 1030
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -