Glycoprotein Synthesis in Plants

Delmer, Deborah P.; Kulow, Carl; Ericson, Mary C.

doi:10.1104/pp.61.1.25

Cited by 45 publications

(13 citation statements)

References 11 publications

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“…Disturbing the sequence of reactions would lead to &1,3 glucan production. Recent evidence of Delmer (30) indicates that cell-free homogenates of cotton fibers have the capacity to synthesize only p-1,3 glucans, even though these cells normally produce largely /3-1,4 cellulosic glucans in vivo.…”

Section: In One Example Brown and Coworkers (4) Demonstrated That Thmentioning

confidence: 99%

Surface architecture of the plant cell: Biogenesis of the cell wall, with special emphasis on the role of the plasma membrane in cellulose biosynthesis

Montezinos

Brown

1976

J Supramol Struct

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Cell wall structure and biogenesis in the unicellular green alga, Oocystis apiculata, is described. The wall consists of an outer amorphous primary layer and an inner secondary layer of highly organized cellulosic microfibrils. The primary wall is deposited immediately after cytokinesis. Golgi-derived products contribute to this layer. Cortical microtubules underlie the plasma membrane immediately before and during primary wall formation. They function in maintaining the elliptical cell shape. Following primary wall synthesis, Golgi-derived materials accumulate on the cell surface to form the periplasmic layer. This layer functions in the deposition of coating and cross-linking substances which associate with cellulosic microfibrils of the incipient secondary wall. Secondary wall microfibrils are assembled in association with the plasma membrane. Freeze-etch preparations of untreated, living cells reveal linear terminal complexes in association with growing cellulosic microfibrils. These complexes are embedded in the EF fracture face of the plasma membrane. The newly synthesized microfibril lies in a groove of the outer leaflet of the plasma membrane. The groove is decorated on the EF fracture face by perpendicular structures termed "ridges". The ridges interlink with definitive rows of particles associated withe PF fracture face of the innter leaflet of the plasma membrane. These particles are termed "granule bands", and they function in the orientation of the newly synthesized microfibrils. Microfibril development in relation to a coordinated multienzyme complex is discussed. The process of cell wall biogenesis in Oocystis is compared to that in higher plants.

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Section: In One Example Brown and Coworkers (4) Demonstrated That Thmentioning

confidence: 99%

Surface architecture of the plant cell: Biogenesis of the cell wall, with special emphasis on the role of the plasma membrane in cellulose biosynthesis

Montezinos

Brown

1976

J Supramol Struct

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“…Vol. 213 Lehle et al, 1976;Brett & Leloir, 1977;Delmer et al, 1978;Chadwick & Northcote, 1980;Staneloni et al, 1980). In the present paper direct evidence is presented regarding the occurrence of dolichol and Dol-P in soya beans.…”

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Characterization of dolichol and dolichyl phosphate phosphatase from soya beans (Glycine max)

Kothapalli¹,

Rip²,

Carroll³

1983

Biochemical Journal

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A series of polyprenols, ranging in length from 15 to 22 isoprene units, has been isolated from soya beans (Glycine max) and purified by high-pressure liquid chromatography. N.m.r., i.r. and mass spectra of the compounds indicated that they are alpha-saturated polyprenols of the dolichol type. The amount present in dry seeds was about 9 mg/100 g, whereas dolichyl phosphate (Dol-P) was present only in trace amounts. Dol-P phosphatase activity was detected in the microsomal fraction of 5-day-old germinating soya-bean cotyledons. The Dol-P phosphatase activity was linear with respect to time and protein concentration and exhibited a broad pH optimum (pH 7-9). Triton X-100 was necessary for significant enzyme activity. Enzyme activity was slightly enhanced by EDTA, whereas dithiothreitol was without effect. An apparent Km of 5 microM was determined for Dol-P. Bivalent metal ions were not required for enzyme activity. A number of phosphorylated compounds tested as enzyme substrates (including a number of nucleoside phosphates, glucose 6-phosphate, sodium beta-glycerophosphate and Na4P2O7) did not compete with [1-3H]Dol-P as substrate. A number of phospholipids were also tested for their ability to act as Dol-P phosphatase substrates. At 1 mM concentration, phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid and lysophosphatidic acid each inhibited enzymic activity. However, at 0.1 mM concentration, phosphatidylcholine and phosphatidylethanolamine were slightly stimulatory, whereas phosphatidic acid and lysophosphatidic acid were still inhibitory. Phosphatidic acid showed competitive inhibition.

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“…Previous studies from our laboratory showed that crude cellfree extracts from this tissue synthesized lipid-linked GlcNAc4, dolichol monophosphoryl mannose, and lipid-oligosaccharide when supplied with UDP-GlcNAc and GDP-mannose, and also transferred GlcNAc and mannose to endogenous acceptor proteins (5,9,10). The lipid-linked sugars showed turnover, consistent with their roles as intermediates in protein glycosylation (9,10).…”

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Two Kinds of Protein Glycosylation in a Cell-Free Preparation from Developing Cotyledons of Phaseolus vulgaris

Davies¹,

Delmer²

1981

Plant Physiol.

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Membrane preparations from developing cotyledons of red kidney bean (Phaseolas vulgaris L) transferred radioactive mannose from GDP-mannose (U-I'4Clmannose) to endogenous acceptor proteins. The transfer was inhibited by the antibiotic tunicamycin, suggesting the involvement of lipidoLigosaccharide intermediates typical of the pathway for glycosylation of asparagine residues. This was supported by the similarity of the linkage types of radioactive mannose in lipid-oligosaccharide and glycoprotein products; both contained labeled 2-linked mannose, 3,6-inked and terminal mannose typical of glycoprotein "core" oligosaccharides. As expected for "core" glycosylation, the transfer of labeled N-acetylgucosamine (GlcNAc) from UDP-GlcNAc (613HIGLcNAc) to 4-linkage in endogenous glycoproteins could also be demonstrated. However, most of the radioactive GlcNAc was incorporated into terminal linkage, in a reaction insensitive to tunicamycin. The proteins receiving "core" oligosaccharide in vitro were heterogeneous in size, in contrast to those receiving most of the GkcNAc (which chiefly comprised the seed reserve-proteins phaseolin and phytohemagglutinin). It is suggested that following "core" glycosylation, single GkcNAc residues are attached terminally to the oligosaccharides of these seed proteins, without the involvement of lipid-linked intermediates. Phaseolin from mature seeds does not possess a significant amount of terminal GIcNAc and so it is possible that these residues are subsequentiy removed in a processing event.cotyledons, is the identity of the endogenous glycoprotein products. Previous studies from our laboratory showed that crude cellfree extracts from this tissue synthesized lipid-linked GlcNAc4, dolichol monophosphoryl mannose, and lipid-oligosaccharide when supplied with UDP-GlcNAc and GDP-mannose, and also transferred GlcNAc and mannose to endogenous acceptor proteins (5, 9, 10). The lipid-linked sugars showed turnover, consistent with their roles as intermediates in protein glycosylation (9, 10). Recently we obtained evidence that the endogenous acceptor proteins for the in vitro transfer of GlcNAc are chiefly the principal reserve proteins of this seed, i.e. phaseolin5 and phytohemagglutinin (4). Both of these proteins contain typical asparagine-linked, "high mannose" type, oligosaccharide groups containing GlcNAc and mannose as sole constituent sugars (10, 17). We therefore expected concomitant incorporation of GlcNAc and mannose, via transfer of "core" oligosaccharides from lipid carriers in the usual pathway (7,22). However, in contrast to the results with GlcNAc, only a trace of incorporation of mannose into phaseolin could be shown (4). We suggested, therefore, the bulk of the transfer of GlcNAc to phaseolin and PHA did not represent "core" glycosylation. In this paper we present confirmatory evidence ofthis, demonstrating that two apparently independent kinds of glycosylation occur in this in vitro system, i.e. the attachment of GlcNAc residues to the identifiable (glyco)proteins phaseol...

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Glycoprotein Synthesis in Plants

Cited by 45 publications

References 11 publications

Surface architecture of the plant cell: Biogenesis of the cell wall, with special emphasis on the role of the plasma membrane in cellulose biosynthesis

Surface architecture of the plant cell: Biogenesis of the cell wall, with special emphasis on the role of the plasma membrane in cellulose biosynthesis

Characterization of dolichol and dolichyl phosphate phosphatase from soya beans (Glycine max)

Two Kinds of Protein Glycosylation in a Cell-Free Preparation from Developing Cotyledons of Phaseolus vulgaris

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