An unambiguous nomenclature for xyloglucan‐derived oligosaccharides

Fry, Stephen C.; York, William S.; Albersheim, Peter; Darvill, Alan G.; Hayashi, Takahisa; Joseleau, J.P.; Kato, Yoji; Lorences, Ester P.; Maclachlan, Gordon; McNeil, Michael; Mort, Andrew J.; Reid, J. S. Grant; Seitz, Hanns Ulrich; Selvendran, Robert R.; Voragen, A.G.J.; White, Alan R.

doi:10.1111/j.1399-3054.1993.tb01778.x

Cited by 468 publications

(156 citation statements)

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“…uronic acid residues) in the xyloglucan itself. To distinguish these possibilities, we applied cellulase, which is expected to digest xyloglucans principally to a series of Glc 4 -based oligosaccharides such as XXFG and XXXG (Fry et al 1993). If acidic residues were present in sucient numbers to give the xyloglucan a perceptible net negative charge, a proportion of the cellulasegenerated oligosaccharides would be anionic.…”

Section: Resultsmentioning

confidence: 99%

Evidence for covalent linkage between xyloglucan and acidic pectins in suspension-cultured rose cells

Thompson

Fry

2000

Planta

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172

102

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Neutral xyloglucan was purified from the cell walls of suspension-cultured rose (Rosa sp. 'Paul's Scarlet') cells by alkali extraction, ethanol precipitation and anion-exchange chromatography on 'Q-Sepharose FastFlow'. The procedure recovered 70% of the total xyloglucan at about 95% purity in the neutral fraction. The remaining 30% of the xyloglucan was anionic, as demonstrated both by anion-exchange chromatography at pH 4.7 and by high-voltage electrophoresis at pH 6.5. Alkali did not cause neutral xyloglucan to become anionic, indicating that the anionic nature of the rose xyloglucan was not an artefact of the extraction procedure. Pre-incubation of neutral [3H]xyloglucan with any of ten non-radioactive acidic polysaccharides did not cause the radioactive material to become anionic as judged by electrophoresis, indicating that stable complexes between neutral xyloglucan and acidic polysaccharides were not readily formed in vitro. The anionic xyloglucan did not lose its charge in the presence of 8 M urea or after a second treatment with NaOH, indicating that its anionic nature was not due to hydrogen-bonding of xyloglucan to an acidic polymer. Proteinase did not affect the anionic xyloglucan, indicating that it was not associated with an acidic protein. Cellulase converted the anionic xyloglucan to the expected neutral nonasaccharide and heptasaccharide, indicating that the repeatunits of the xyloglucan did not contain acidic residues. Endo-polygalacturonase converted about 40% of the anionic xyloglucan to neutral material. Arabinanase and galactanase also converted appreciable proportions of the anionic xyloglucan to neutral material. These results show that about 30% of the xyloglucan in the cell walls of suspension-cultured rose cells exists in covalently-linked complexes with acidic pectins.

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Section: Resultsmentioning

confidence: 99%

Evidence for covalent linkage between xyloglucan and acidic pectins in suspension-cultured rose cells

Thompson

Fry

2000

Planta

Self Cite

172

102

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“…The XGps or XGos content of samples was determined by the same assay, using a known amount of bean XGos as a standard. (Fry et al 1993) specifying the sidechain substitution pattern for each b-D-glucosyl residue in the xyloglucan backbone is shown below the structure. XGps is cleaved by endoglucanases such as cellulase or XEG that hydrolyze the XGps backbone at the unsubstituted b-D-glucosyl residues (arrows), yielding XGos…”

Section: Colorimetric Assaysmentioning

confidence: 99%

Effects of the mur1 mutation on xyloglucans produced by suspension-cultured Arabidopsis thaliana cells

Pauly

Eberhard

Albersheim

et al. 2001

Planta

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Mutation of the Arabidopsis thaliana (L.) Heynh. gene MUR1, which encodes an isoform of GDP-D-mannose-4,6-dehydratase, affects the biosynthetic conversion of GDP-mannose to GDP-fucose. Cell walls in the aerial tissues of mur1 plants are almost devoid of alpha-L-fucosyl residues, which are partially replaced by closely related alpha-L-galactosyl residues. A line of suspension-cultured A. thaliana cells was generated from leaves of mur1 plants and the structure of the xyloglucan in the walls of these cells was structurally characterized. Xyloglucan fractions were prepared from the walls of both wild-type (WT) and mur1 cells by sequential extraction with a xyloglucan-specific endoglucanase (XEG) and aqueous KOH. Structural analysis of these fractions revealed that xyloglucan produced by cultured mur1 cells is similar, but not identical to that isolated from leaves of mur1 plants. As previously reported for mur1 leaves, the xyloglucan from cultured mur1 cells contains less than 5% of the fucose present in the xyloglucan from WT cells. Fucosylation of the xyloglucan is substantially restored when mur1 cells are grown in medium supplemented with L-fucose. Xyloglucan isolated from leaves contains more oligosaccharide subunits in which the central sidechain is terminated with a beta-D-galactosyl residue than does xyloglucan prepared from cultured cells. This was observed for both mur1 and WT plants, indicating that this correlation is independent of the mur1 mutation and that it is possible to distinguish changes due to genetic mutation from those due to the physiological state of the cells in culture. Suspension-cultured cells thus provide a convenient source of genetically altered cell wall material, facilitating the biochemical characterization of mutations that affect cell wall structure.

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“…The XGOs relevant to this paper are shown in Fig. 1 and named using the structural nomenclature of Fry et al (1993).…”

Section: Assay On Pea Xgosmentioning

confidence: 99%

α-Fucosidases with different substrate specificities from two species of Fusarium

Paper

Scott-Craig

Cavalier

et al. 2012

Appl Microbiol Biotechnol

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Two fungal-secreted α-fucosidases and their genes were characterized. FoFCO1 was purified from culture filtrates of Fusarium oxysporum strain 0685 grown on L-fucose and its encoding gene identified in the sequenced genome of strain 4287. FoFCO1 was active on p-nitrophenyl-α-fucoside (pNP-Fuc), but did not defucosylate a nonasaccharide (XXFG) fragment of pea xyloglucan. A putative α-fucosidase gene (FgFCO1) from Fusarium graminearum was expressed in Pichia pastoris. FgFCO1 was ~1,800 times less active on pNP-Fuc than FoFCO1, but was able to defucosylate the XXFG nonasaccharide. Although FgFCO1 and FoFCO1 both belong to Glycosyl Hydrolase family 29, they share <25 % overall amino acid identity. Alignment of all available fungal orthologs of FoFCO1 and FgFCO1 indicated that these two proteins belong to two subfamilies of fungal GH29 α-fucosidases. Fungal orthologs of subfamily 1 (to which FoFCO1 belongs) are taxonomically more widely distributed than subfamily 2 (FgFCO1), but neither was universally present in the sequenced fungal genomes. Trichoderma reesei and most species of Aspergillus lack genes for either GH29 subfamily.

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An unambiguous nomenclature for xyloglucan‐derived oligosaccharides

Cited by 468 publications

References 0 publications

Evidence for covalent linkage between xyloglucan and acidic pectins in suspension-cultured rose cells

Evidence for covalent linkage between xyloglucan and acidic pectins in suspension-cultured rose cells

Effects of the mur1 mutation on xyloglucans produced by suspension-cultured Arabidopsis thaliana cells

α-Fucosidases with different substrate specificities from two species of Fusarium

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