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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 80 (1990), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Leaf thionins of barley have been identified as a novel class of highly abundant polypeptides with antifungal activity, which are present in walls and vacuoles of barley leaf cells. Similar thionins occur not only in monocotyledonous but also in various dicotyledonous plants. The leaf thionins of barley are encoded by a complex multigene family, which consists of at least 50–100 members per haploid genome. The toxicity of these thionins for plant pathogenic fungi and the fact that their synthesis can also be triggered by pathogens strongly suggest that leaf thionins are involved in the mechanism of plant defence against microbiol infection.
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 69 (1987), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The photoreduction of protochlorophyllide was studied in leaves and isolated chloroplasts of barley. Leaves of plants which had been preilluminated for varying lengths of time were incubated with [14C]-δ- aminolevulinic acid for 2 h in the dark. The subsequent photoreduction of [14C]-protochlorophyllide was analyzed by high performance liquid chromatography of pigments extracted from illuminated leaves and plastids. The plastids used in this study were isolated in the dark from leaves at the end of the 2 h labelling period. Three major results were obtained:〈list xml:id="l1" style="custom"〉1The extent of protochlorophyllide reduction in vivo was rapidly reduced as a function of the preillumination period. In 24 h preilluminated plants only a small fraction of the radioactively labelled protochlorophyllide was reduced during the subsequent light period.2The amount of NADPH-protochlorophyllide oxidoreductase (EC 1.6.99.-) present in plastids of fully-green plants was drastically reduced relative to levels in plastids of dark-grown plants as estimated by the methods of immunoblotting of plastid proteins and immunogold labelling of ultrathin sections of the leaf tissue.3In etiolated plants light seemed to affect the reduction of protochlorophyllide directly through the excitation of protochlorophyllide. In fully green plants, however, light also affected chlorophyll formation indirectly by the supply of NADPH via photosynthetic electron transport.
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 64 (1985), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In recent years there has been a considerable increase in our understanding of the manner by which light affects gene expression during chloroplast development. In most systems that have been studied, light acts through sensitive photoreceptor molecules and quantitatively increases or represses the level of expression of specific nuclear-and plastid-encoded genes. Although the mechanisms are obscure, a picture is beginning to emerge in which the coordination of nuclear and plastid gene expression is controlled by regulatory mechanisms originating within their respective subcellular compartments. This review summarizes some of our current knowledge concerning the nature of light-regulated gene expression in higher plants and provides a prospectus for future research in this area.
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  • 4
    ISSN: 1432-2048
    Keywords: Chloroplast development ; Hordeum (chlorophyll accumulation) ; Light, chloroplast development ; NADPH-protochlorophyllide oxidoreductase ; Protochlorophyllide/chlorophyllide conversion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The possible regulatory role of NADPH-protochlorophyllide oxidoreductase for chlorophyll accumulation has been investigated in barley plants. Within the primary leaf of etiolated plants the different maturation stages of etioplasts are found in a linear series with the youngest in cells near the base and the oldest in cells near the tip. This distribution of different plastid forms is paralleled by drastic differences in the NADPH-protochlorophyllide-oxidoreductase content of the plastids and their capacity to accumulate chlorophyll during illumination. The amount of enzyme and the rate of chlorophyll accumulation are highest in the mature etioplast in the tip of the leaf and both decline rapidly with decreasing age of the leaf tissue, being almost undetectable in the leaf base. The translatable mRNA coding for the enzyme shows a different distribution pattern within the leaf. The highest concentration is found in the middle part of the leaf while in the top part only traces of this mRNA are detectable. It is concluded that during leaf development the enzyme is synthesized rapidly only during a limited time period and that it is stored subsequently in the mature etioplast as a stable protein. The close correlation between the distribution of the enzyme within the barley leaf and that of the potential to accumulate chlorophyll during illumination would favour a control of chlorophyll accumulation by the amount of NADPH-protochlorophyllide oxidoreductase. Dark-grown plants which were exposed to far-red light were used to test this possibility. The far-red-absorbing form of phytochrome (Pfr) has an inverse effect on the kinetics of chlorophyll accumulation and the enzyme concentration. Our results indicate that the rate of chlorophyll accumulation in barley is not determined by the level of NADPH-protochlorophyllide oxidoreductase present in the leaves.
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  • 5
    ISSN: 1432-2048
    Keywords: Hordeum ; NADPH-protochlorophyllide oxidoreductase (site of synthesis) ; Plastid ribosomes ; Ribosomes (plastid) ; Temperature and plastid ribosomes deficiency
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract High-temperature-induced deficiency of plastid ribosomes in barley plants (Hordeum vulgare L.) was used as a system for studying the role of the cytoplasm in the synthesis of the NADPH-protochlorophyllide oxidoreductase. The enzyme is present in 33° C-grown plants. The failure of high-temperature-grown plants to accumulate chlorophyll during illumination is not caused by the absence of the protochlorophyllide-reducing enzyme. The synthesis of the NADPH-protochlorophyllide oxidoreductase was studied by feeding [35S]methionine to the seedling and by following the incorporation of the radioactively labeled amino acid into plastid proteins. The NADPH-protochlorophyllide oxidoreductase was labeled in high-temperature-grown barley plants to the same extent as in control plants grown at 25° C. It is concluded that the 36,000-Mr polypeptide of the NADPH-protochlorophyllide oxidoreductase is synthesized outside the plastid on cytoplasmic 80S ribosomes.
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  • 6
    ISSN: 1432-2048
    Keywords: Hordeum (P700 apoprotein synthesis) ; Photosystem I ; P700 apoprotein ; Phytochrome and P700 apoprotein synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract This work reports on the regulation of synthesis of the P700 chlorophyll-a apoprotein of photosystem I in barley. The mRNA for the P700 apoprotein is almost exclusively confined to the plastid membrane-bound polysomes. However, the mRNA for the 32-kDa herbicide-binding protein of photosystem II is found in both the soluble and membrane-bound polysomes. The mRNA for the P700 apoprotein is found in similar amounts in dark-grown and light-grown wild-type as well as mutant xantha-l81 barley. The latter mutant is deficient in chlorophyll biosynthesis. However, while wild-type leaves accumulate the P700 chlorophyll-a protein only in the light, mutant leaves never accumulate the P700 apoprotein. A more sensitive approach was taken using isolated plastids to study P700 apoprotein synthesis. Etioplasts did not synthesize detectable P700 apoprotein even when the etioplasts were exposed to light. However, only a 1-min exposure of leaves to light was necessary to induce P700 apoprotein synthesis by isolated plastids. Phytochrome involvement in controlling P700 apoprotein synthesis was tested by using red/farred light treatment of leaves. These treatments showed no far-red reversibility of red-induced P700-apoprotein synthesis in isolated plastids even after 3 h of darkness after the light treatments. From these data we conclude that the accumulation of P700 apopootein is not under the control of phytochrome and that the light induction of P700 apoprotein is most likely mediated through the protochlorophyllide/chlorophyllide system. This control, however, may also involve cytoplasmic signals as the synthesis of the P700 apoprotein is not turned on in illuminated etioplasts.
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  • 7
    ISSN: 1432-2048
    Keywords: Chloroplast ; Light-harvesting chlorophyll a/b protein ; Photosynthesis (low light) ; Pith ; Populus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Pith cells of young poplar (Populus x canadensis Moench) twigs were found to contain chlorophylls a and b. In addition, it was shown that pith cells also have a considerable amount of light-harvesting chlorophyll a/b protein (LHCP), which was identified by Western blotting and localized by immunogold labelling of ultrathin sections. The data strongly indicate that these cells, though they are completely covered by wood and bark and thus are accessible only to very low amounts of light, possess a functionally active photosynthetic apparatus. Evidence for this was found by feeding isolated longitudinal sections of pith with radioactively labelled carbon dioxide and exposing them to light. After incubation, reduced carbohydrates could be detected by thinlayer chromatography, indicating that photosynthesis occurs.
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  • 8
    ISSN: 1432-2048
    Keywords: Hordeum (plastid transformation) ; Light and etioplast transformation ; Protochlorophyllide oxidoreductase ; Proteolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The role of proteolysis during the light-induced rapid decrease of the NADPH: protochlorophyllide oxidoreductase in barley was studied. A proteolytic activity with a pH optimum of 4.5 was present in a plastid preparation of etiolated barley seedlings. No other proteolytic activity could be detected. The temperature optimum for the proteolysis was 50°C, and the highest specific activity was measured with hemoglobin as the substrate. In contrast to previous proposals, no evidence for the specific involvement of this protease was found during the light-induced transformation of etioplasts to chloroplasts.
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  • 9
    ISSN: 1432-2048
    Keywords: Hordeum ; NADPH-protochlorophyllide oxidoreductase ; Polypeptide (amount, light-induced changes)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Seedlings of barley were grown either in continuous darkness or under a diurnal 12 h light/12 h dark cycle and the effects on NADPH-protochlorophyllide oxidoreductase were followed at two different levels. Firstly, the relative content of the mRNA encoding the NADPH-protochlorophyllide oxidoreductase was measured by dot-blot hybridization. Secondly, changes in the enzyme polypeptide were monitored either by the method of immunoblotting or by immunogold labelling of ultrathin sections of Lowicryl-embedded leaf tissue. Our results demonstrate that drastic diurnal changes in the level of mRNA sequences and the enzyme protein are unlikely to occur in plants which have been grown under natural light/dark conditions. In the dark, protein and mRNA accumulation occurs at an early developmental stage. These results are difficult to reconcile with the suggestion that the massive accumulation of mRNA and enzyme protein in dark-grown seedlings is primarily the consequence of an artificially extended darkperiod. In addition to the plastid-specific NADPH-protochlorophyllide oxidoreductase a closely related polypeptide has been detected outside the plastid in the surrounding cytoplasm (Dehseh et al. 1986b, Planta 169, 172–183). During the diurnal light/dark treatment of seedlings the concentrations of the two protein populations did not show any variation indicative of an exchange between the two protein populations across the plastid envelope.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Planta 173 (1988), S. 31-34 
    ISSN: 1432-2048
    Keywords: Populus ; Protein body ; Protein storage ; Ray cell ; Vacuole
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Light- and electron-microscopical investigations revealed distinct intravacuolar protein aggregates of 0.3–0.8 μm in diameter in ray cells of poplar during the dormant season. In semi-thin sections, these bodies showed positive protein staining and enzymatic digestibility with pepsin, indicating their proteinaceous nature. Morphometric measurements showed such protein bodies in 7–13% of the area of the ray-cell lumen. This amount corresponded with the protein content of the wood determined biochemically, e.g. 2.0–5.0 μg·mg-1 dry weight. Polyacrylamide gel electrophoresis of the total protein fraction extracted from wood showed prominent polypeptide species with an apparent molecular weight of 30–32 kilodaltons. The results indicate considerable protein storage in ray cells, especially in the form of protein-storage vacuoles.
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