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[Polysaccharides of flower plants: structure and physiological activity].

The results of studies on the chemical structure and physiological activity of phanerogam polysaccharides, accumulated within the last two decades, are reviewed. Three types of polysaccharides are considered: rhamnogalacturonans (pectins and related gums and mucilages, type A), acidic arabinogalactans (mainly plant mucilages, gums, and some hemicelluloses, type B), and neutral glucans and heteroglycans (reserve polysaccharides, type C). Various physiological activities of these plant polysaccharides are discussed, with particular emphasis being placed on their immunomodulatory action. The data available on the relationship between chemical structure and physiological activity of plant polysaccharides are considered. Information on the medicinal use of some plants containing physiologically active polysaccharides is presented.

Adjuvants, Immunologic↗

Insect antifeedants from tropical plants: structures of dumnin and dumsenin.

Two novel A-seco limonoids, dumnin and dumsenin, were isolated from the methanolic extract of Croton jatrophoides by bioassay-guided fractionation, and the structures were determined by nuclear magnetic resonance, circular dichroism, and mass spectrometry experiments. These compounds showed potent antifeedant activity (PC(50) <or= 2.0 microg/mL) against the larvae of pink bollworm, Pectinophora gossypiella, and/or fall armyworm, Spodoptera frugiperda, providing results comparable to dumsin and zumsin, previously isolated from the same plant.

Animals↗

Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants--structural and kinetic properties of the free and bound enzymes.

The last steps of cysteine synthesis in plants involve two consecutive enzymes. The first enzyme, serine acetyltransferase, catalyses the acetylation of L-serine in the presence of acetyl-CoA to form O-acetylserine. The second enzyme, O-acetylserine (thiol) lyase, converts O-acetylserine to L-cysteine in the presence of sulfide. We have, in the present work, over-produced in Escherichia coli harboring various type of plasmids, either a plant serine acetyltransferase or this enzyme with a plant O-acetylserine (thiol) lyase. The free recombinant serine acetyltransferase (subunit mass of 34 kDa) exhibited a high propensity to form high-molecular-mass aggregates and was found to be highly unstable in solution. However, these aggregates were prevented in the presence of O-acetylserine (thiol) lyase (subunit mass of 36 kDa). Under these conditions homotetrameric serine acetyltransferase associated with two molecules of homodimeric O-acetylserine (thiol) lyase to form a bienzyme complex (molecular mass approximately 300 kDa) called cysteine synthase containing 4 mol pyridoxal 5'-phosphate/mol complex. O-Acetylserine triggered the dissociation of the bienzyme complex, whereas sulfide counteracted the action of O-acetylserine. Protein-protein interactions within the bienzyme complex strongly modified the kinetic properties of plant serine acetyltransferase: there was a transition from a typical Michaelis-Menten model to a model displaying positive kinetic co-operativity with respect to serine and acetyl-CoA. On the other hand, the formation of the bienzyme complex resulted in a very dramatic decrease in the catalytic efficiency of bound O-acetylserine (thiol) lyase. The latter enzyme behaved as if it were a structural and/or regulatory subunit of serine acetyltransferase. Our results also indicated that bound serine acetyltransferase produces a build-up of O-acetylserine along the reaction path and that the full capacity for cysteine synthesis can only be achieved in the presence of a large excess of free O-acetylserine (thiol) lyase. These findings contradict the widely held belief that such a bienzyme complex is required to channel the metabolite intermediate O-acetylserine.

Acetyltransferases↗

The use of an optical brightener in the study of plant structure.

An optical brightener Calcoflour White M2R New has been used to stain cell walls of higher plants. It can be used either as a vital stain for intact plants or for hand sections and plastic-embedded thin sections. Walls are brilliantly fluorescent while most cytoplasmic components are normally unstained. The brightener binds strongly to cellulose, carboxylated polysaccharides, and callose. Staining for 20 sec to 2 min in a 0.01% solution of the brightener is preferred for most purposes.

Cell Wall↗

Leucine-rich repeat receptor kinases in plants: structure, function, and signal transduction pathways.

Leucine-rich repeat receptor kinases (LRR-RKs) comprise the largest subfamily of transmembrane receptor-like kinases in plants, with over 200 members in Arabidopsis. LRR-RKs regulate a wide variety of developmental and defense-related processes including cell proliferation, stem cell maintenance, hormone perception, host-specific as well as non-host-specific defense response, wounding response, and symbiosis. Several studies indicate that LRR-RKs act as dimers, and some may form a receptor complex with leucine-rich repeat receptor-like proteins (LRR-RPs) that lack a cytoplasmic kinase domain. Despite the fact that structural features of LRR-RKs are fairy similar, five available ligand molecules for LRR-RKs are structurally diverse, from steroids (brassinolides) to peptides (phytosulfokine and systemin) and secreted proteins (CLV3). Precise ligand-binding sites of LRR-RKs are not understood. However, the extracellular "island" domain that intercepts the LRR domain in some LRR-RKs may play an important role in ligand binding. Advances in unveiling components of three LRR-RK signaling pathways, namely BRI1 in steroid signaling, CLV1 in meristem maintenance, and FLS2 in bacterial elicitor perception, revealed an intriguing link between plant LRR-RK and animal receptor signaling pathways. Finally, rapid progress made in LRR-RK research beyond the model system Arabidopsis has provided exciting, novel insights into the evolution of the LRR-RK signaling system in plants, such as BRI1 utilized in the wound-responsive signaling pathway in Solanaceae plants and recruitment of CLV1 in nodule development in leguminous plants.

Binding Sites↗

Characterization of antibodies against methyl-pppN cap structure: plant U3 small nucleolar RNA is recognized by these antibodies.

In eukaryotes, many small nuclear RNAs contain either a trimethylguanosine cap structure of a gamma-monomethyl (me) cap structure. Previously, we reported the characterization of anti-mepppG antibodies which recognize methyl-capped RNAs with G as the initiation nucleotide. We report here the preparation of antibodies against mepppN cap structure. Anti-mepppN antibodies recognized only mepppN from a mixture of mepppN and pppN and immunoprecipitated mepppA-capped U3 small nucleolar RNA from a mixture of cowpea cell RNAs. These anti-mepppN antibodies recognized methylated nucleoside triphosphates (mepppA, mepppC, mepppG and mepppU) with nearly equal efficiency; however, these antibodies did not recognize methyl phosphate or methylated mononucleotides. These antibodies will be useful in the identification and characterization of all methyl-capped RNAs no matter which is the initiation nucleotide.

Antibodies, Antinuclear↗

Vacuolar H(+)-translocating ATPases from plants: structure, function, and isoforms.

The vacuolar H(+)-translocating ATPase (V-type ATPase) plays a central role in the growth and development of plant cells. In a mature cell, the vacuole is the largest intracellular compartment, occupying about 90% of the cell volume. The proton electrochemical gradient (acid inside) formed by the vacuolar ATPase provides the primary driving force for the transport of numerous ions and metabolites against their electrochemical gradients. The uptake and release of solutes across the vacuolar membrane is fundamental to many cellular processes, such as osmoregulation, signal transduction, and metabolic regulation. Vacuolar ATPases may also reside on endomembranes, such as Golgi and coated vesicles, and thus may participate in intracellular membrane traffic, sorting, and secretion. Plant vacuolar ATPases are large complexes (400-650 kDa) composed of 7-10 different subunits. The peripheral sector of 5-6 subunits includes the nucleotide-binding catalytic and regulatory subunits of approximately 70 and approximately 60 kDa, respectively. Six copies of the 16-kDa proteolipid together with 1-3 other subunits make up the integral sector that forms the H+ conducting pathway. Isoforms of plant vacuolar ATPases are suggested by the variations in subunit composition observed among and within plant species, and by the presence of a small multigene family encoding the 16-kDa and 70-kDa subunits. Multiple genes may encode isoforms with specific properties required to serve the diverse functions of vacuoles and endomembrane compartments.

Amino Acid Sequence↗

LEA proteins in higher plants: structure, function, gene expression and regulation.

Late embryogenesis abundant (LEA) proteins are mainly low molecular weight (10-30 kDa) proteins, which are involved in protecting higher plants from damage caused by environmental stresses, especially drought (dehydration). These findings and the fact that the breeding of drought tolerant varieties would be of great value in agriculture, form the basis of search for anti-drought inducible genes and their characterization. LEA proteins are generally classified into six groups (families) according to their amino acid sequence and corresponding mRNA homology, which are basically localized in cytoplasm and nuclear region. LEA protein synthesis, expression and biological activities are regulated by many factors (e.g. developmental stages, hormones, ion change and dehydration), signal transduction pathways and lea genes. No tissue-specific lea gene expression has been considered as one main regulatory mechanism on the basis of extensive studies with the model plant, Arabidopsisthaliana. The study of the regulatory mechanism of lea gene expression is an important feature of modern plant molecular biology.

Arabidopsis↗

BORON IN PLANT STRUCTURE AND FUNCTION.

New and exciting developments in boron research in the past few years greatly contributed to better understanding of the role of boron in plants. Purification and identification of the first boron-polyol transport molecules resolved much of the controversy about boron phloem mobility. Isolation and characterization of the boron-polysaccharide complex from cell walls provided the first direct evidence for boron crosslinking of pectin polymers. Inhibition and recovery of proton release upon boron withdrawal and restitution in plant culture medium demonstrated boron involvement in membrane processes. Rapid boron-induced changes in membrane function could be attributed to boron-complexing membrane constituents. Boron may affect metabolic pathways by binding apoplastic proteins to cis-hydroxyl groups of cell walls and membranes, and by interfering with manganese-dependent enzymatic reactions. In addition, boron has been implicated in counteracting toxic effects of aluminum on root growth of dicotyledonous plants. Molecular investigations of boron nutrition have been initiated by the discovery of a novel mutant of Arabidopsis thaliana with an altered requirement for boron.

Journal Article↗

Organochlorine compounds from a terrestrial higher plant: structures and origin of chlorinated orcinol derivatives from diseased bulbs of Lilium maximowiczii.

Seven chlorine-containing orcinol derivatives (2-8) and orcinol (9) have been isolated from diseased bulbs of the edible lily Lilium maximowiczii, and their structures have been elucidated. Six of the chlorinated orcinol derivatives (2, 4-8) showed antifungal activity. Because organochlorine compounds are rare in terrestrial higher plants, their biosynthetic origin was examined. These compounds were shown to be induced in intact bulb scales by UV irradiation or by inoculation with the pathogenic fungus Fusarium oxysporum f. sp. lilii. Biosynthetic studies suggested that these "natural organochlorine pesticides" are produced by enzymatic chlorination of orcinol (9) with chloroperoxidase and hydrogen peroxide, which are both induced in the plant tissue under stress conditions.

Antifungal Agents↗

The use of ethylenediamine in softening hard plant structures for paraffin sectioning.

Ethylenediamine has been used as an agent for softening very hard woods prior to sectioning on a sliding microtome. The use of ethylenediamine is recommended for two additional uses: for preparing 1) soft woods in which wide, thin-walled tracheids or vessels tend to collapse during sliding microtome sectioning and 2) plant tissues with sclerenchyma mixed with soft-walled cells (bark, leaves, fruits, etc.) which frequently fail to section well. After softening in ethylenediamine, material is washed, infiltrated, and embedded in paraffin. Preliminary sections are made with a rotary microtome, just exposing the cut surface of the material; this exposed surface is soaked overnight in water. Sectioning is then continued. Sections produced in this fashion are considerably improved. The wood and pith of Podocarpus ustus, a parasitic conifer from New Caledonia, is used as an object to demonstrate improvements in sectioning by the ethylenediamine-paraffin method. Thinner sections with minimal tearing, cell collapse, and unevenness are produced. Sections can be handled easily and stained more effectively than unmounted sections. Variations in timing and in treatment are recommended to suit different materials. Ethylenediamine, used with reasonable caution, is much less hazardous than hydrofluoric acid and is more effective in softening plant material. The ethylenediamine method may be used routinely on any material difficult to section because of hardness.

Ethylenediamines↗

First 2-hydroxy-3-methylbut-3-enyl substituted xanthones isolated from plants: structure elucidation, synthesis and antifungal activity.

Two new 2-hydroxy-3-methylbut-3-enyl substituted xanthones, (+/-)-caledol 1 and (+/-)-dicaledol 2 were isolated from a dichloromethane extract of the leaves of Calophyllum caledonicum (Clusiaceae). Compounds 1 and 2 are the first 2-hydroxy-3-methylbut-3-enyl substituted xanthones isolated from natural source. Their structures were elucidated by means of combined analytical methods including HRFABMS, 1D and 2D NMR spectroscopies and also confirmed by total synthesis using biomimetic ortho-prenylphenols photooxygenation (1O2) as a key step. The antifungal activity against Aspergillus fumigatus is reported.

Aspergillus fumigatus↗