Abstract
The importance of threonine in the Asn-X-Thr recognition sequence for asparagine-linked glycosylation was tested by examining the effect of a threonine analog, beta-hydroxynorvaline, on co-translational glycosylation in Krebs' II ascites tumor lysates. beta-Hydroxynorvaline inhibited the glycosylation of the alpha subunit of human chorionic gonadotropin and the beta subunit of bovine luteinizing hormone; both proteins contain Asn-X-Thr recognition sites. The effect was prevented by threonine, indicating that beta-hydroxynorvaline acted via its incorporation into protein. These results provide direct evidence for the role of threonine in Asn-X-Thr sites for asparagine-linked glycosylation. The results support the view that this site is sensitive to steric hindrance.
| Original language | English |
|---|---|
| Pages (from-to) | 8007-8010 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 255 |
| Issue number | 17 |
| State | Published - Sep 10 1980 |