Inhibition of asparagine-linked glycosylation by incorporation of a threonine analog into nascent peptide chains.

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.

• Authors: G Hortin, I Boime
• Journal: The Journal of biological chemistry (J Biol Chem) Vol. 255 Issue 17 Pg. 8007-10 (Sep 10 1980) ISSN: 0021-9258 [Print] United States
• PMID: 6773934 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Chorionic Gonadotropin
• Glycosides
• RNA, Messenger
• Tunicamycin
• 3-hydroxynorvaline
• Threonine
• Asparagine
• Luteinizing Hormone

Topics

• Animals
• Asparagine (metabolism)
• Carcinoma, Krebs 2 (metabolism)
• Cattle
• Chorionic Gonadotropin (biosynthesis)
• Glycosides (metabolism)
• Humans
• Intracellular Membranes (metabolism)
• Luteinizing Hormone (biosynthesis)
• Mice
• Microsomes (drug effects, metabolism)
• Peptide Biosynthesis
• Protein Biosynthesis (drug effects)
• RNA, Messenger (metabolism)
• Threonine (analogs & derivatives, metabolism, pharmacology)
• Tunicamycin (pharmacology)