Detection, biosynthesis and some functions of glycans N-linked to plant secreted proteins

Faye, Loı̈c; Fitchette-Lainé, Anne-Catherine; Gomord, Véronique; Chekkafi, Aicha; Delaunay, A; Driouich, Azeddine

doi:10.1017/cbo9780511600401.016

Cited by 17 publications

(21 citation statements)

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“…By comparing the effects of different elicitor molecules, we demonstrated also that the extent ofimmobilisation is dependent on the level of the H202 production as well as on the degree of pH changes evoked by elicitor. Immobilisation is confined to a small subset of proteins, mainly (hydroxy)prolinecontaining glycoproteins, while glycoproteins with N-linked oligosaccharide side chains remain unchanged, indicating the importance of the type of glycosylation on the stability and function of wall proteins under stress conditions and in development [22]. Analysis of hydroxyproline content in the wall proteins indicated that only a limited number of proteins contained hydroxylated proline and that they were grouped in two regions, 90-200 kDa and 30-45 kDa.…”

Section: Discussionmentioning

confidence: 99%

Specificity in the immobilisation of cell wall proteins in response to different elicitor molecules in suspension-cultured cells of French bean (Phaseolus vulgaris L.)

1995

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A characteristic of the defence response is the immobilisation of wall proteins possibly through the formation of covalent cross-links and the subsequent barrier formation against pathogens. A requirement for this is the generation of active oxygen species, particularly hydrogen peroxide. In the present work, we examine in depth the requirement for H2O2 and the specificity of the immobilisation with respect to particular wall proteins. Salt-extractable wall proteins were analysed for hydroxyproline content and the subset of proteins with this post-translational modification was found to be small. About 50 proteins were found to be easily salt-extractable and in response to elicitor treatment about 5 were found to be specifically immobilised. Immobilisation was very rapid and completed within 15 min after elicitation, and dependent upon the type of elicitor and the intensity of the production of active oxygen species. N-terminal sequencing and amino acid analysis revealed that, apart from one polypeptide, all immobilised proteins were (hydroxy)proline-containing glycoproteins with O-linked oligosaccharide side chains. In contrast, N-linked glycoproteins were not immobilised. N-terminal protein sequencing revealed the immobilised HRGPs to be novel, but both extensin and PRP-like. Implications of these findings for both pathogenic and symbiotic processes are also discussed.

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Section: Discussionmentioning

confidence: 99%

Specificity in the immobilisation of cell wall proteins in response to different elicitor molecules in suspension-cultured cells of French bean (Phaseolus vulgaris L.)

1995

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“…In higher plants, inhibition of N-glycosylation by tunicamycin has been shown to lead to a rapid intracellular proteolysis of the secretory proteins (Ravi et al 1986;Driouich et al 1989;Faye and Chrispeels 1989), whereas most vacuolar proteins are correctly targeted to the vacuole (for review, see Faye et al 1993). Recently, it was demonstrated that glycoprotein secretion in plants Fig.…”

Section: Discussionmentioning

confidence: 99%

The Golgi apparatus of the scaly green flagellate Scherffelia dubia : uncoupling of glycoprotein and polysaccharide synthesis during flagellar regeneration

Perasso

Grunow

Bruntrup

et al. 2000

Planta

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The flagella of the green alga Scherffelia dubia are covered by scales which consist of acidic polysaccharides and glycoproteins. Experimental deflagellation results in the regeneration of flagella complete with scales. During flagellar regeneration, scales are newly synthesized in the Golgi apparatus, exocytosed and deposited on the growing flagella. Flagellar regeneration is dependent upon protein synthesis and N-glycosylation, as it is blocked by cycloheximide and partially inhibited by tunicamycin. Metabolic labeling with [35S]methionine/cysteine demonstrated that scale-associated proteins were not newly synthesized during flagellar regeneration, suggesting that the proteins deposited on regenerating flagella were drawn from a pool. Quantitative immunoelectron microscopy using a monospecific antibody directed against a scale-associated protein of 126 kDa (SAP126) revealed that the pool of SAP126 was primarily located at the plasma membrane, with minor labeling of the scale reticulum and trans-Golgi cisternae, both before deflagellation and during flagellar regeneration. Since SAP126 was sequestered during flagellar regeneration into secretory vesicles together with newly synthesized scales, it is concluded that the persistent presence of SAP126 in the trans-Golgi cisternae during scale biogenesis requires retrograde transport of the protein from the plasma membrane to the Golgi apparatus.

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“…The removal of the signal peptide is the first necessary step that a secretory protein must undergo to acquire its correct conformation (Helenius et al, 1992); further modifications do usually include N-Glycosylation (Faye et al, 1993) folding, via the formation of both non-covalent and covalent bonds within the protein, and assembly, via the formation of intermolecular interactions between polypeptides (reviewed by Vitale and Denecke, 1999).…”

Section: The Synthesis and Processing Of Prolamins Occur In The Ermentioning

confidence: 99%

Trafficking and deposition of prolamins in wheat

Tosi

2012

Journal of Cereal Science

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Detection, biosynthesis and some functions of glycans N-linked to plant secreted proteins

Cited by 17 publications

References 0 publications

Specificity in the immobilisation of cell wall proteins in response to different elicitor molecules in suspension-cultured cells of French bean (Phaseolus vulgaris L.)

Specificity in the immobilisation of cell wall proteins in response to different elicitor molecules in suspension-cultured cells of French bean (Phaseolus vulgaris L.)

The Golgi apparatus of the scaly green flagellate Scherffelia dubia : uncoupling of glycoprotein and polysaccharide synthesis during flagellar regeneration

Trafficking and deposition of prolamins in wheat

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