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