Activation of cell wall-associated peroxidase isoenzymes in pea epicotyls by a xyloglucan-derived nonasaccharide

Warneck, H.; Haug, Thomas; Seitz, Hanns Ulrich

doi:10.1093/jxb/47.12.1897

Cited by 23 publications

(13 citation statements)

References 29 publications

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“…In contrast to this, all types of oligosaccharides used were without any effect on the soluble peroxidases activity (unpublished results). Our results are comparable with xyloglucan nonasaccharide action which increased the activity of cell wallassociated peroxidases at the same time as it caused growth inhibition (Warneck et al 1996). This inverse correlation between peroxidase activity and elongation growth is widely accepted (Bagatharia & Chanda 1998;Schopfer 2001, Dunand et al 2003.…”

Section: Resultssupporting

confidence: 88%

“…2 after 2,4-D action. Cationic isoperoxidases are probably predominant isozymes in pea epicotyl cell walls (Warneck et al 1996). These isoperoxidases are in general connected with indoleacetic acid degradation which is linked with the oxidation of suitable co-substrates such as phenolic compounds and catalysis of the linkages between phenolic acids and cell-wall polymers (Wallace & Fry 1999).…”

Section: Resultsmentioning

confidence: 99%

“…Isolation of intracellular and cell wall-associated peroxidases fraction from pea epicotyl segments was carried out as described by Warneck et al (1996). Pea epicotyl segments of each treatment in the bioassay were homogenized in liquid nitrogen with mortar and pestle, suspended in 0.1 M TRIS HCl buffer (pH 7.0) and homogenized again by ultrasonication (6 × 60 s, 21.5 kHz) on ultrasonic generator UG 252.…”

Section: Peroxidase Extraction and Detectionmentioning

confidence: 99%

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Galactoglucomannan oligosaccharides inhibition of elongation growth is in pea epicotyls coupled with peroxidase activity

et al. 2009

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The effect of galactoglucomannan oligosaccharides -GGMOs, GGMOs-r (GGMOs with reduced reducing ends), and GGMOs-g (GGMOs with reduced number of D-galactose units) on peroxidase activity was determined in pea epicotyls. GGMOs didn't significantly modify the activity of soluble peroxidases. However, cell wall-associated peroxidases activity increased after GGMOs and GGMOs-r treatment, while in the presence of GGMOs-g this activity was significantly lower. These results are inversely related to the GGMOs, GGMOs-r, and GGMOs-g effect on elongation growth induced by 2,4-D (2,4-dichlorophenoxyacetic acid) in pea epicotyls. It can be concluded that GGMOs evoked inhibition of the elongation growth induced by auxin is probably associated with cell wall modifications catalysed by peroxidase.Key words: 2,4-D; elongation growth; galactoglucomannan oligosaccharides; pea epicotyls; peroxidases Abbreviations: 2,4-D, 2,4-dichlorophenoxyacetic acid; d.p., degree of polymerisation; GGMOs, galactoglucomannan oligosaccharides; GGMOs-g, galactoglucomannan oligosaccharides with reduced number of D-galactose units; GGMOs-r, galactoglucomannan oligosaccharides with reduced reducing ends.

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Section: Resultssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

Section: Peroxidase Extraction and Detectionmentioning

confidence: 99%

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Galactoglucomannan oligosaccharides inhibition of elongation growth is in pea epicotyls coupled with peroxidase activity

et al. 2009

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“…In fact, plant peroxidases have been reported to inhibit cell elongation by catalyzing cross linking of phenolic groups and proteins such as extensins 20,60 or compounds like ferulic acid, monolignol and aliphatic components. 19,[61][62][63] The short and long hypocotyl phenotypes found in AtPRX53 overexpression and atprx53 mutant lines, respectively, provide strong support for the hypothesis that AtPRX53 could catalyze the cross linking of cell wall compounds to modulate, or potentially counteract, cell elongation. Such a role also makes sense with regard to the expression of AtPRX53 in the ©2 0 1 1 L a n d e s B i o s c i e n c e .…”

Section: Methodsmentioning

confidence: 72%

Arabidopsis peroxidase AtPRX53 influences cell elongation and susceptibility toHeterodera schachtii

Jin

Hewezi

Baum

2011

Plant Signaling & Behavior

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“…The reported inhibitory effect of the fucose-containing oligosaccharide may result not from a direct interaction with XET but instead from a signal transduction cascade, such as the induction of wall-associated peroxidase (35) and͞or ␣-fucosidase activities (36).…”

Section: Discussionmentioning

confidence: 99%

Suppression and acceleration of cell elongation by integration of xyloglucans in pea stem segments

Takeda

Furuta

Awano

et al. 2002

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

184

141

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Xyloglucan is a key polymer in the walls of growing plant cells. Using split pea stem segments and stem segments from which the epidermis had been peeled off, we demonstrate that the integration of xyloglucan mediated by the action of wall-bound xyloglucan endotransglycosylase suppressed cell elongation, whereas that of its fragment oligosaccharide accelerated it. Whole xyloglucan was incorporated into the cell wall and induced the rearrangement of cortical microtubules from transverse to longitudinal; in contrast, the oligosaccharide solubilized xyloglucan from the cell wall and maintained the microtubules in a transverse orientation. This paper proposes that xyloglucan metabolism controls the elongation of plant cells.X yloglucan, which occurs widely in the primary walls of higher plants, possesses a 1,4-␤-glucan backbone with 1,6-␣-xylosyl residues along the backbone. Because the 1,4-␤-glucan backbone can bind specifically to cellulose microfibrils by hydrogen bonds (1), the xyloglucan probably contributes to the rigidity of the cell wall by cross-linking adjacent microfibrils (2). In fact, microfibrils seem to be coated with xyloglucan, which is located both on and between microfibrils throughout cell elongation (3). Masking xyloglucans in cell walls should prevent xyloglucan metabolism; in agreement with this prediction, an antibody specific to xyloglucan prevented an auxin-induced decrease in molecular size of xyloglucan and inhibited indole-3-acetic acid (IAA)-induced cell elongation in azuki hypocotyl segments (4). Xyloglucan endotransglycosylase (XET) has been proposed to participate in the dynamic changes of xyloglucan cross-linking (5, 6), but there is little direct evidence for this hypothesis. The question at issue concerns the structural function of xyloglucan, namely whether xyloglucan contributes to the extensibility of the wall by cross-linking adjacent microfibrils.Fucose-containing xyloglucan oligosaccharides have been shown to inhibit auxin-induced elongation of pea stems (7,8). Their inhibitory activity is approximately maximal at a concentration of 10 Ϫ8 to 10 Ϫ9 M. In the absence of auxin, a high concentration (Ͼ10 Ϫ8 M) of xyloglucan oligosaccharide did not inhibit but slightly promoted cell elongation in pea stem segments (9). Thus, the oligosaccharides may provide either negative or positive feedback control during cell elongation. However, the positive feedback reaction has not been reproducibly observed in pea stems (T.T. and T.H., unpublished results) and also was not observed in maize primary roots (10). In the present communication, we examine whether xyloglucan oligosaccharides control the elongation growth of plant cells.In cylindrical plant organs such as roots or stems, cells expand anisotropically, with the direction of most rapid growth parallel to the long axis of the organ, leading to elongation of the organ. It has been known for many years that the direction of elongation is perpendicular to the direction of net orientation of cellulose microfibrils (11). Therefore, paral...

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Activation of cell wall-associated peroxidase isoenzymes in pea epicotyls by a xyloglucan-derived nonasaccharide

Cited by 23 publications

References 29 publications

Galactoglucomannan oligosaccharides inhibition of elongation growth is in pea epicotyls coupled with peroxidase activity

Galactoglucomannan oligosaccharides inhibition of elongation growth is in pea epicotyls coupled with peroxidase activity

Arabidopsis peroxidase AtPRX53 influences cell elongation and susceptibility toHeterodera schachtii

Suppression and acceleration of cell elongation by integration of xyloglucans in pea stem segments

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