Xyloglucans in the Primary Cell Wall

Hayashi, Takahisa

doi:10.1146/annurev.pp.40.060189.001035

Cited by 755 publications

(354 citation statements)

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“…We were able to express both AtCSLC4 and TmCSLC genes in P. pastoris, as was done earlier for AtXT1 to characterize its xylosyltransferase activity (4). We also coexpressed AtXT1 and AtCSLC4 in P. pastoris, because there is evidence that xylosyltransferase and GS act together during XyG biosynthesis (2,4). Thus, we postulated that xylosyltransferase (AtXT1) might be required to stimulate the putative GS activity.…”

Section: Resultsmentioning

confidence: 99%

“…Methylation analyses were performed in triplicate on three different cultures; results were averaged and expressed as Ϯ SD. 2 ) data for standard cellohexaose (G6) and purified G5-R molecules were obtained by using a Thermo Electron vMALDI (Thermo Electron, Santa Clara, CA). Preparation of G6 and G5-R molecules is detailed in SI Text.…”

Section: (See Si Text)mentioning

confidence: 99%

“…It has a ␤-1,4-glucan backbone that is substituted in a regular pattern with xylosyl residues plus other sugars that vary depending on the plant species (2). Although considerable progress has been made in defining the structure and the biological functions of XyG (1,2), its biosynthesis is poorly understood. It is known to be synthesized in the Golgi of plants cells before delivery to the cell surface and incorporation into the wall matrix (3).…”

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confidence: 99%

“…Efforts to identify the GS responsible for XyG biosynthesis by traditional methods of protein purification have not been successful (2,8). Because of the structural similarity between the ␤-linked glycan chains of matrix polysaccharides and the ␤-linked glucan chains of cellulose, the cellulose synthase-like (CSL) genes have been suggested as likely candidates for encoding the Golgi-localized glycan synthases involved in matrix polysaccharide biosynthesis (9), including the GS required for XyG biosynthesis.…”

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confidence: 99%

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A gene from the cellulose synthase-like C family encodes a β-1,4 glucan synthase

Cocuron

Lerouxel

Drakakaki

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

292

265

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Despite the central role of xyloglucan (XyG) in plant cell wall structure and function, important details of its biosynthesis are not understood. To identify the gene(s) responsible for synthesizing the ␤-1,4 glucan backbone of XyG, we exploited a property of nasturtium (Tropaeolum majus) seed development. During the last stages of nasturtium seed maturation, a large amount of XyG is deposited as a reserve polysaccharide. A cDNA library was produced from mRNA isolated during the deposition of XyG, and partial sequences of 10,000 cDNA clones were determined. A single member of the C subfamily from the large family of cellulose synthase-like (CSL) genes was found to be overrepresented in the cDNA library. Heterologous expression of this gene in the yeast Pichia pastoris resulted in the production of a ␤-1,4 glucan, confirming that the CSLC protein has glucan synthase activity. The Arabidopsis CSLC4 gene, which is the gene with the highest sequence similarity to the nasturtium CSL gene, is coordinately expressed with other genes involved in XyG biosynthesis. These and other observations provide a compelling case that the CSLC gene family encode proteins that synthesize the XyG backbone.nasturtium ͉ cell wall ͉ xyloglucan ͉ polysaccharide

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Section: Resultsmentioning

confidence: 99%

Section: (See Si Text)mentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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A gene from the cellulose synthase-like C family encodes a β-1,4 glucan synthase

Cocuron

Lerouxel

Drakakaki

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

292

265

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“…It hydrogen-bonds to, and probably tethers, neighbouring microfibrils [9][10][11][12]. It was therefore of interest to investigate whether xyloglucan chains undergo transglycosylation in the walls of living plant cells.…”

Section: Introductionmentioning

confidence: 99%

Xyloglucan undergoes interpolymeric transglycosylation during binding to the plant cell wall in vivo: evidence from 13C/3H dual labelling and isopycnic centrifugation in caesium trifluoroacetate

Thompson

Smith

Fry

1997

Biochemical Journal

105

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Xyloglucan from the walls of Rosa cells that had been cultured on [12C]- or [13C]-glucose formed bands in caesium trifluoroacetate with mean buoyant densities of 1.575 or 1.616 g/ml respectively. Incubation of a mixture of [13C,3H]xyloglucan and [12C,1H]xyloglucan in the presence of xyloglucan endotransglycosylase (XET) activity caused the mean buoyant density of the radioactive material to decrease, indicating that interpolymeric transglycosylation could be detected in vitro. We used two 13C/3H-dual-labelling protocols to look for interpolymeric transglycosylation in vivo. In protocol A, [13C]glucose-grown Rosa cells were transferred into [12C]glucose medium 6 h after a ≈ 2 h pulse of L-[1-3H]arabinose (which radiolabels the xylose residues of xyloglucan). The mean buoyant density of the wall-bound [3H]xyloglucan decreased during the following 7 days in culture. This indicates that, during or after the wall-binding of newly synthesized [12C,1H]xyloglucan, it became covalently attached to previously wall-bound [13C,3H]xyloglucan. In protocol B, [12C]glycerol- or [12C]glucose-grown Rosa cells were transferred into [13C]glucose medium, 20 or 60 min before a ≈ 2 h pulse of [3H]arabinose. The buoyant density of the earliest wall-bound [3H]xyloglucan showed that it had a 12C/13C ratio of ~ 1:1. This indicates that, during (or, implausibly, before) wall-binding, the newly synthesized [13C,3H]xyloglucan became covalently attached to previously synthesized [12C]xyloglucan. During the following 7 days in culture, the mean buoyant density of the [3H]xyloglucan increased, showing that later-synthesized [13C,1H]xyloglucan can be covalently attached to previously wall-bound [12C,13C,3H]xyloglucan. The only known mechanism by which segments of xyloglucans could become covalently attached to each other in the cell wall is by interpolymeric transglycosylation catalysed by XET. We conclude that XET-catalysed interpolymeric transglycosylation accompanies, and probably causes, the integration of newly secreted xyloglucan into the cell-wall architecture.

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A conformational study of the xyloglucan oligomer, XXXG, by NMR spectroscopy and molecular modeling

et al. 2000

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Xyloglucans in the Primary Cell Wall

Cited by 755 publications

References 58 publications

A gene from the cellulose synthase-like C family encodes a β-1,4 glucan synthase

A gene from the cellulose synthase-like C family encodes a β-1,4 glucan synthase

Xyloglucan undergoes interpolymeric transglycosylation during binding to the plant cell wall in vivo: evidence from 13C/3H dual labelling and isopycnic centrifugation in caesium trifluoroacetate

A conformational study of the xyloglucan oligomer, XXXG, by NMR spectroscopy and molecular modeling

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