Book contents
- Frontmatter
- Contents
- List of contributors
- List of abbreviations
- Preface
- Some roles of post-translational modifications in plants
- Signal transduction and protein phosphorylation in bacteria
- Roles of protein phosphorylation in animal cells
- The significance of post-translational modification of proteins by phosphorylation in the regulation of plant development and metabolism
- Post-translational modification of chloroplast proteins and the regulation of protein turnover
- Purification of a small phosphoprotein from chloroplasts and characterisation of its phosphoryl group
- Use of synthetic peptides to study G proteins and protein kinases within plant cells
- Activation of membrane-associated protein kinase by lipids, its substrates, and its function in signal transduction
- Distribution and function of Ca2+-dependent, calmodulin-independent protein kinases
- Phosphorylation of the plasma membrane proton pump
- The regulation of phosphoenolpyruvate carboxylase by reversible phosphorylation
- Protein phosphorylation and circadian rhythms
- Control of translation by phosphorylation of mRNP proteins in Fucus and Xenopus
- Regulation of plant metabolism by reversible protein (serine/threonine) phosphorylation
- Detection, biosynthesis and some functions of glycans N-linked to plant secreted proteins
- Biosynthesis, intracellular transport and processing of ricin
- Post-translational processing of concanavalin A
- The role of cell surface glycoproteins in differentiation and morphogenesis
- Ubiquitination of proteins during floral development and senescence
- Index
Detection, biosynthesis and some functions of glycans N-linked to plant secreted proteins
Published online by Cambridge University Press: 06 July 2010
- Frontmatter
- Contents
- List of contributors
- List of abbreviations
- Preface
- Some roles of post-translational modifications in plants
- Signal transduction and protein phosphorylation in bacteria
- Roles of protein phosphorylation in animal cells
- The significance of post-translational modification of proteins by phosphorylation in the regulation of plant development and metabolism
- Post-translational modification of chloroplast proteins and the regulation of protein turnover
- Purification of a small phosphoprotein from chloroplasts and characterisation of its phosphoryl group
- Use of synthetic peptides to study G proteins and protein kinases within plant cells
- Activation of membrane-associated protein kinase by lipids, its substrates, and its function in signal transduction
- Distribution and function of Ca2+-dependent, calmodulin-independent protein kinases
- Phosphorylation of the plasma membrane proton pump
- The regulation of phosphoenolpyruvate carboxylase by reversible phosphorylation
- Protein phosphorylation and circadian rhythms
- Control of translation by phosphorylation of mRNP proteins in Fucus and Xenopus
- Regulation of plant metabolism by reversible protein (serine/threonine) phosphorylation
- Detection, biosynthesis and some functions of glycans N-linked to plant secreted proteins
- Biosynthesis, intracellular transport and processing of ricin
- Post-translational processing of concanavalin A
- The role of cell surface glycoproteins in differentiation and morphogenesis
- Ubiquitination of proteins during floral development and senescence
- Index
Summary
Introduction
When considering the first steps in plant glycobiology, summarised in this review, it may be wise not to forget the suggestion of a French philosopher about the period that precedes attempts at addressing a new issue:
L'important est plus de poser les vraies questions que d'apporter les vraies réponses.
Levi-StraussLaboratories interested in plant glycobiology are currently asking some very basic questions such as:
What is a plant glycoprotein glycan made of?
How is a peptide glycosylated?
How is an N-linked glycan processed in a plant cell?
Why are some plant proteins N-glycosylated?
The present review is an attempt to summarise the way these questions are being addressed and the preliminary answers that have already been obtained.
Structures of N-linked glycans
Plant glycoproteins have oligosaccharide sidechains attached to their protein backbone via an N-linkage (amide nitrogen of asparagine) or O-linkage (hydroxyl group of serine, threonine or hydroxyproline). The N-linked oligosaccharides, or glycans, found on plant glycoproteins fall into two general categories already described for other eukaryotes: highmannose and complex glycans. The high-mannose type oligosaccharides have the general structure Man5–9(GlcNAC)2. High-mannose type oligosaccharides are found associated with immature and mature glycoproteins of higher plants (Faye et al., 1986). High-mannose glycans, first described for soybean lectin (Lis & Sharon, 1978), were observed in many other mature, vacuolar or extracellular plant lectins and enzymes (Paul & Stigbrand, 1970; Ericson & Chrispeels, 1973; Basha & Beevers, 1976; Sturm et al., 1987a).
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- Post-translational Modifications in Plants , pp. 213 - 242Publisher: Cambridge University PressPrint publication year: 1993
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