Relationship of coniferin β-glucosidase to lignification in various plant cell suspension cultures

Hösel, Wolfgang; Fiedler-Preiss, Anette; Borgmann, Edith

doi:10.1007/bf02318912

Cited by 31 publications

(9 citation statements)

References 32 publications

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“…P-Glucosidases capable of hydrolyzing coniferin have been detected in suspension culture systems (Hosel and Todenhagen, 1980;Hosel et al, 1982) and seedlings (Marcinowski and Grisebach, 1978), but, to our knowledge, a coniferin glucosidase has not been idektified that derives from differentiating xylem of mature trees, the most active site for lignin biosynthesis in woody plants.…”

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confidence: 97%

A [beta]-Glucosidase from Lodgepole Pine Xylem Specific for the Lignin Precursor Coniferin

1995

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Coniferin, the glucoside of the monolignol coniferyl alcohol, accumulates to high levels in gymnosperms during spring-cambial reactivation. A cinnamyl alcohol glucoside/P-glucosidase system is thought to play a key role i n lignification by releasing the monolignol aglycones. lnvestigation of such an enzyme system in the xylem of Pinus contorta var latifolia Engelm. revealed two major P-glucosidases. One efficiently hydrolyzed the native substrate, coniferin, and the other was more active against synthetic glucosides. l h e coniferin P-glucosidase was purified to apparent homogeneity using anion exchange, hydrophobic interaction, and size-exclusion chromatography. The apparent native molecular weight was estimated to be 60,000. A dominant 28-kD protein and a minor 24-kD protein were detected in the purified preparation following sodium dodecyl sulfate-polyacrylamide gel electrophoresis. lmmunological evidence from polyclonal antibodies directed against the synthetic N-terminal peptide of the 24-kD protein suggested that the native protein is a dimer of 28-kD subunit size. The N-terminal sequence showed that coniferin P-glucosidase has high homology to known plant P-glucosidases. Coniferin, syringin, and a synthetic coniferin analog were preferred substrates for the coniferin 6-glucosidase. In situ localization using the chromogenic coniferin analog showed the exclusive presence of P-glucosidase activity in the differentiating xylem, similar to peroxidase activity.

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confidence: 97%

A [beta]-Glucosidase from Lodgepole Pine Xylem Specific for the Lignin Precursor Coniferin

1995

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“…In soybean (Glycine max), a b-glucosidase in vitro specific for coniferin, syringin, and ferulic acid 4-O-b-D-glucoside has been isolated (Hosel and Todenhagen, 1980). In cell suspension cultures of Petroselinum hortense and wheat (Triticum aestivum), the appearance of b-glucosidase activity is correlated with the initiation of lignification and, sometimes, with the appearance of other enzymes involved in lignin biosynthesis (Hosel et al, 1982).…”

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Impact of the Absence of Stem-Specific β-Glucosidases on Lignin and Monolignols

et al. 2012

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Monolignol glucosides are thought to be implicated in the lignin biosynthesis pathway as storage and/or transportation forms of cinnamyl alcohols between the cytosol and the lignifying cell walls. The hydrolysis of these monolignol glucosides would involve b-glucosidase activities. In Arabidopsis (Arabidopsis thaliana), in vitro studies have shown the affinity of b-GLUCOSIDASE45 (BGLU45) and BGLU46 for monolignol glucosides. BGLU45 and BGLU46 genes are expressed in stems. Immunolocalization experiments showed that BGLU45 and BGLU46 proteins are mainly located in the interfascicular fibers and in the protoxylem, respectively. Knockout mutants for BGLU45 or BGLU46 do not have a lignin-deficient phenotype. Coniferin and syringin could be detected by ultra-performance liquid chromatography-mass spectrometry in Arabidopsis stems. Stems from BGLU45 and BGLU46 mutant lines displayed a significant increase in coniferin content without any change in coniferyl alcohol, whereas no change in syringin content was observed. Other glucosylated compounds of the phenylpropanoid pathway were also deregulated in these mutants, but to a lower extent. By contrast, BGLU47, which is closely related to BGLU45 and BGLU46, is not implicated in either the general phenylpropanoid pathway or in the lignification of stems and roots. These results confirm that the major in vivo substrate of BGLU45 and BGLU46 is coniferin and suggest that monolignol glucosides are the storage form of monolignols in Arabidopsis, but not the direct precursors of lignin.

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“…Some authors suggested that the rate and the location of lignification are controlled by these β-glucosidases. 184 However, it is still unclear whether coniferin and other glucosylated monolignols are obligate precursors of lignin. In 1933, Erdtman 185 proposed that monolignols are polymerized into lignin by an oxidative mechanism involving free-radical intermediates.…”

Section: Generalities and Biosynthesismentioning

confidence: 99%