Glycosylated and phosphorylated proteins - Expression in yeast and oocytesof Xenopus: Prospects and challenges - Relevance to expression of thermostable proteins

Citation
Pz. Li et al., Glycosylated and phosphorylated proteins - Expression in yeast and oocytesof Xenopus: Prospects and challenges - Relevance to expression of thermostable proteins, PROT EX PUR, 22(3), 2001, pp. 369-380
Citations number
149
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PROTEIN EXPRESSION AND PURIFICATION
ISSN journal
10465928 → ACNP
Volume
22
Issue
3
Year of publication
2001
Pages
369 - 380
Database
ISI
SICI code
1046-5928(200108)22:3<369:GAPP-E>2.0.ZU;2-6
Abstract
Phosphorylation and glycosylation are important posttranslational events in the biosynthesis of proteins. The different degrees of phosphorylation and glycosylation of proteins have been an intriguing phenomenon. Advances in genetic engineering have made it possible to control the degree of glycosyl ation and phosphorylation of proteins. Structural biology of phosphorylated and glycosylated proteins has been advancing at a much slower pace due to difficulties in using high-resolution NMR studies in solution phase. Major difficulties have arisen from the inherent mobilities of phosphorylated and glycosylated side chains. This paper reviews molecular and structural biol ogy of phosphorylated and glycosylated proteins expressed in eukaryotic exp ression systems which are especially suited for large-scale production of t hese proteins. In our laboratory, we have observed that eukaryotic expressi on systems are particularly suited for the expression of thermostable light -activated proteins, e.g., bacteriorhodopsins and plastocyanins. (C) 2001 A cademic Press.