Hydroxyproline Metabolism during Mungbean and Soya-bean Seedling Growth1

Chao, Hai-Yen; Dashek, William V.

doi:10.1093/oxfordjournals.aob.a084686

Cited by 15 publications

(4 citation statements)

References 7 publications

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“…In addition to hydroxyproline arabinosides, hydroxyproline O-galactoside has been found in alkaline extracts of cell-wall preparations of Chlamydomonas reinhardtii (Miller et al, 1972;Roberts et al, 1972) and Lamport et al (1973) reported that serine O-galactosides are present in tomato cell walls. Other investigators have noted that hydroxyproline-rich material is present in 'cytoplasmic' fractions (Clarke et al, 1968;Cleland, 1968;Jennings & Watt, 1967;Pusztai & Watt, 1969;Lamport, 1970;Chao & Dashek, 1973) in addition to cell-wall fractions.…”

Section: Discussionmentioning

confidence: 97%

Chemical and physical properties of an arabinogalactan-peptide from wheat endosperm

Fincher¹,

Sawyer²,

Stone³

1974

Biochemical Journal

144

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1. An arabinogalactan-peptide from wheat endosperm was studied by using physicochemical techniques and some aspects of its chemical structure were determined. 2. The arabinogalactan-peptide is a non-associating, polydisperse macromolecule ([unk]=22000) which exhibits only minor non-ideal effects in aqueous solution. 3. Examination of the products of partial acid hydrolysis of the polysaccharide component showed that arabinose is present in the alpha-l-arabinofuranosyl configuration, and i.r.-absorption spectroscopy and optical-rotation studies suggest that the d-galactopyranose residues are linked by glycosidic linkages in the beta-anomeric configuration. 4. The arabinogalactan is linked to a peptide which represents 8% (w/w) of the arabinogalactan-peptide and which may be present as a molecular core. Partial degradation of the polymer by successive treatment with oxalic acid and NaOH showed that the linkage between polysaccharide and peptide involves galactose and hydroxyproline residues and is glycosidic in nature. A tentative model is proposed for the structure of the wheat endosperm arabinogalactan-peptide. 5. The subcellular location and function of the arabinogalactan-peptide is discussed in relation to previous work with related molecules.

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Section: Discussionmentioning

confidence: 97%

Chemical and physical properties of an arabinogalactan-peptide from wheat endosperm

Fincher¹,

Sawyer²,

Stone³

1974

Biochemical Journal

144

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“…Its level varies somewhat, depending on the plant or organ considered (6,28) but, with the exception of some organisms like Chlamydomonas (29), it is generally low. This level is markedly increased in a few instances where the integrity of the plant is disrupted by wounding, aeration of tissue slices (8), subculturing, and in melon plants infected by a fungal pathogen (16).…”

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confidence: 99%

Cell Surfaces in Plant-Microorganism Interactions

Esquerré-Tugayé¹,

Lafitte²,

Mazau³

et al. 1979

Plant Physiol.

185

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Enrichment of the cell wal in hydroxyproline-rich glycoprotein is involved in the defense of muskmelon (Cucumis melo) seedings to CoUetotriclwm lagenarium, the causative agent of anthracnose. The extent to which this accumulation proceeds may be experimentally modified by treating plants with ethylene or growing them in the presence of free Ltrans-hydroxyproline. It appears that the increase in the wail hydroxyproline-rich glycoprotein mediated through ethylene is paralleled by an increasing resistance of the host to the pathogen. Inversely, inhibiting the synthesis of this glycoprotein in diseased plants is strictly correlated to an accelerated and more intense colonization of the host by the pathogen.In both cases, the inverse relationship between the accumulation of hydroxyproline-rich glycoproteins and the ability of the pathogen to develop in the host has been checked by the quantification, in infected tissues, of glucosamine, a characteristic component of chitin-containing fungi.It has been shown that hydroxyproline is associated with the cell wall of green plants (23)(24)(25). Its level varies somewhat, depending on the plant or organ considered (6, 28) but, with the exception of some organisms like Chlamydomonas (29), it is generally low. This level is markedly increased in a few instances where the integrity of the plant is disrupted by wounding, aeration of tissue slices (8), subculturing, and in melon plants infected by a fungal pathogen (16). The observed increase in diseased plants accounts for a cell wall enrichment of the glycosylated hydroxyprolyl and seryl residues (15) which typify the hydroxyprolinerich glycoprotein (HRGP)3 called "extensin" by Lamport (23).The question of the significance of this glycoprotein accumulation in diseased plants has been raised, particularly because cell surface glycoconjugates are often involved in cell to cell interactions (4, 10, 35) of which the host-pathogen system is a special case. This paper reports on the correlations between the level of HRGP in the cell wall, and the extent of pathogen spread in melon plants infected by Colletotrichum lagenarium. The approach to this problem consisted of modifying the hydroxyproline level 'This work received financial support from the Centre National de la Recherche Scientifique (L.A. n°241).

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“…These (glyco)peptides include the galactosylcontaining pentapeptide, serine-hydroxyproline4. This pentapeptide is characteristic of cell wall protein.Some aspects of the biosynthesis (4,5,27) and secretion (6) of this glycoprotein have also been studied.The present paper partially characterizes the macromolecules responsible for the 10-fold increase in hydroxyproline which occurs in the cell walls of fungal infected melon plants (10,28). This increase was formerly shown to be coincident with an increase in hydroxyproline arabinosides (12), to be dependent on protein synthesis (1 1) and paralleled by a concomitant enrichment of the wall in proteins (10, 28).…”

mentioning

confidence: 99%

“…Some aspects of the biosynthesis (4,5,27) and secretion (6) of this glycoprotein have also been studied.…”

mentioning

confidence: 99%

Cell Surfaces in Plant-Microorganism Interactions

Esquerré-Tugayé

Lamport

1979

Plant Physiol.

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Infection of muskmelon Cueumis mclo seedlings by the fungus CoHletotrchum lagenarinm causes a 10-fold increase in the amount of cell wail hydroxyproline-rich glycoprotein. Evidence for this increase was provided by studying two specific markers of this glycoprotein, namely hydroxyproline and glycosylated serine. The lability of the O-glycosidic linkage of wall-bound glycosylated serine in the presence of hydrazine, was used to determine the amount of serine which is glycosylated.A large increase in the hydroxyproline content of infected plants isshown, but the ratios of glycosylated serine to hydroxyproline are similar in healthy and infected plants. As far as these markers are concerned, the hydroxyproline-rich glycoproteins secreted into the wail as a result of the disease are similar to those of healthy plants. In addition, the extent of glycosylation of the wail serine, in both healthy and infected plants, decreases as the plant ages.Serine-and hydroxyproline-rich (glyco)peptides were also isolated after trypsinolysis of the wail. These (glyco)peptides include the galactosylcontaining pentapeptide, serine-hydroxyproline4. This pentapeptide is characteristic of cell wall protein.Some aspects of the biosynthesis (4,5,27) and secretion (6) of this glycoprotein have also been studied.The present paper partially characterizes the macromolecules responsible for the 10-fold increase in hydroxyproline which occurs in the cell walls of fungal infected melon plants (10,28). This increase was formerly shown to be coincident with an increase in hydroxyproline arabinosides (12), to be dependent on protein synthesis (1 1) and paralleled by a concomitant enrichment of the wall in proteins (10, 28). These findings suggested that the synthesis of HRGP is enhanced in diseased plants. The possibility that these molecules could be unique was raised by their higher extent of hydroxyproline glycosylation than in healthy plants (12).For glycosylation of a protein to occur, the glycosyl transferases must recognize a sequence of amino acids (34). The experiments reported below were designed to determine whether the observed increased glycosylation of hydroxyproline might reflect a modification in the sequence of the amino acids at the glycosylation sites. Analyses were undertaken of the amino acid residues known to be in the vicinity of the hydroxyproline arabinosides of the wall. Hydroxyproline, serine, and particularly the ratios of glycosylated serine to total hydroxyproline were thus determined during the course of the disease and during natural aging. Hydroxyproline-rich (glyco)peptides were also isolated, with the aim of determiig their amino acid sequence.Hydroxyproline is an integral component of plant cell wall macromolecules (2,7,25,26,31, 32). It can account for up to 20%Yo of the wall amino acid residues in suspension cultured cells and is found in a hydroxyproline-rich glycoprotein (HRGP)2 that has been called "extensin" (19,20 CELL WALL GLYCOPROTEIN IN INFECTED PLANTSsodium salts, distilled H20, and acetone as...

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Hydroxyproline Metabolism during Mungbean and Soya-bean Seedling Growth1

Cited by 15 publications

References 7 publications

Chemical and physical properties of an arabinogalactan-peptide from wheat endosperm

Chemical and physical properties of an arabinogalactan-peptide from wheat endosperm

Cell Surfaces in Plant-Microorganism Interactions

Cell Surfaces in Plant-Microorganism Interactions

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