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  • 1
    Electronic Resource
    Electronic Resource
    Microdistribution of manganese in the leaf tissues of different plant species as revealed by X-ray microanalyzer (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 53 (1981), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Microdistribution patterns of Mn in the leaf tissues of 9 plant species, Quercus mongolica Fisch. var. grosseserrata Rehd. et Wils., Lindera erythrocarpa Makino, Rhus trichocarpa Miq., Ilex crenata Thunb. var paludosa (Nakai) Hara, Acer sieboldianum Miq., Acanthopanax sciadophylloides Franch. et Savat., Clethra barbinervis Sieb. et Zucc., Pieris japonica (Thunb.) D. Don and Rhododendron semibarbatum Maxim. were studied by means of a wavelength dispersive type X-ray microanalyzer in conjunction with cryostage. The results showed that Mn, in general, was highly concentrated in the epidermal, palisade and spongy parenchyma cells of the leaf tissues of the investigated plants with optimal Mn supply.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1981.tb04491.x
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  • 2
    Electronic Resource
    Electronic Resource
    Thioredoxin h is one of the major proteins in rice phloem sap (1995)
    Springer
    Planta 195 (1995), S. 456-463 
    Details
    ISSN: 1432-2048
    Keywords: Oryza (phloem proteins) ; Phloem sap ; protein ; Sieve tube ; Thioredoxin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sieve tubes play important roles in the transfer of nutrients as well as signals. Hundreds of proteins were found in pure phloem sap collected from rice (Oryza sativa L. cv. Kantou) plants through the cut ends of insect stylets. These proteins may be involved in nutrient transfer and signal transduction. To characterize the nature of these proteins, the partial amino-acid sequence of a 13kDa protein, named RPP13-1, that was abundant in the pure phloem sap was determined. A cDNA clone of 687 bp, containing an open reading frame of 122 amino acids, was isolated using corresponding oligonucleotides as a probe. The deduced amino-acid sequence was very similar to that of the ubiquitous thiol redox protein, thioredoxin. The consensus sequences of thioredoxins are highly conserved. No putative signal peptide was identified. Antiserum against wheat thioredoxin h cross-reacted with RPP13-1 in the phloem sap of rice plants. RPP131 produced in Escherichia coli was reactive to antiserum against wheat thioredoxin h. Both E. coli-produced RPP13-1 and the phloem sap proteins catalyzed the reduction of the disulfide bonds of insulin in the presence of dithiothreitol. These results indicate that an active thioredoxin is a major protein translocating in rice sieve tubes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00202605
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of immunologically related proteins in sieve-tube exudate collected from monocotyledonous and dicotyledonous plants (1998)
    Springer
    Planta 206 (1998), S. 245-252 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Actin filament ; Companion cell-sieve element complex ; Phloem sap proteins ; Plasmodesmal trafficking ; Protease inhibitor ; Protein folding ; Redox regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The mature, functional sieve-tube system in higher plants is dependent upon protein import from the companion cells to maintain a functional long-distance transport system. Soluble proteins present within the sieve-tube lumen were investigated by analysis of sieve-tube exudates which revealed the presence of distinct sets of polypeptides in seven monocotyledonous and dicotyledonous plant species. Antibodies directed against sieve-tube exudate proteins from Ricinus communis L. demonstrated the presence of shared antigens in the phloem sap collected from Triticum aestivum L., Oryza sativa L., Yucca filamentosa L., Cucurbita maxima Duch., Robinia pseudoacacia L. and Tilia platyphyllos L. Specific antibodies were employed to identify major polypeptides. Molecular chaperones related to Rubisco-subunit-binding protein and cyclophilin, as well as ubiquitin and the redox proteins, thioredoxin h and glutaredoxin, were detected in the sieve-tube exudate of all species examined. Actin and profilin, a modulator of actin polymerization, were also present in all analyzed phloem exudates. However, some proteins were highly species-specific, e.g. cystatin, a protease-inhibitor was present in R. communis but was not detected in exudates from other species, and orthologs of the well-known squash phloem lectin, phloem protein 2, were only identified in the sieve-tube exudate of R. communis and R. pseudoacacia. These findings are discussed in terms of the likely roles played by phloem proteins in the maintenance and function of the enucleate sieve-tube system of higher plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050396
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  • 4
    Electronic Resource
    Electronic Resource
    Rice phloem thioredoxin h has the capacity to mediate its own cell-to-cell transport through plasmodesmata (1998)
    Springer
    Planta 205 (1998), S. 12-22 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Companion cell-sieve tube system ; Nicotiana ; Oryza (phloem thioredoxin) ; Phloem function ; Plasmodesmata (protein trafficking) ; Thioredoxin (mutants)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Rice (Oryza sativa L.) phloem sieve tubes contain RPP13-1, a thioredoxin h protein that moves around the plant via the translocation stream. Such phloem-mobile proteins are thought to be synthesized in the companion cells prior to being transferred, through plasmodesmata, to the enucleate sieve-tube members. In this study, in-situ hybridization experiments confirmed that expression of RPP13-1 is restricted to companion cells within the mature phloem. To test the hypothesis that RPP13-1 enters the sieve tube, via plasmodesmata, recombinant RPP13-1 was expressed in Escherichia coli, extracted, purified and fluorescently labeled with fluorescein isothiocyanate (FITC) for use in microinjection experiments into tobacco (Nicotiana tabacum L.) mesophyll cells. The FITC-RPP13-1 moved from the injected cell into surrounding cells, whereas the E. coli thioredoxin, an evolutionary homolog of RPP13-1, when similarly labeled and injected, failed to move in this same experimental system. In addition, co-injection of RPP13-1 and FITC-dextrans established that RPP13-1 can induce an increase in plasmodesmal size exclusion limit to a value greater than 9.4 but less than 20 kDa. Nine mutant forms of RPP13-1 were constructed and tested for their capacity to move from cell to cell; two such mutants were found to be incapable of movement. Crystal-structure prediction studies were performed on wild-type and mutant RPP13-1 to identify the location of structural motifs required for protein trafficking through plasmodesmata. These studies are discussed with respect to plasmodesmal-mediated transport of macromolecules within the companion cell-sieve tube complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050291
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  • 5
    Electronic Resource
    Electronic Resource
    Role of O-acetyl-l-serine in the coordinated regulation of the expression of a soybean seed storage-protein gene by sulfur and nitrogen nutrition (1999)
    Springer
    Planta 209 (1999), S. 282-289 
    Details
    ISSN: 1432-2048
    Keywords: Key wordsO-Acetyl-l-serine ; Arabidopsis (transgenic) ; β-Conglycinin (β-subunit) ; Glycine (storage protein) ; Storage protein ; Sulfur deficiency
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The composition of seed storage proteins is regulated by sulfur and nitrogen supplies. Under conditions of a low sulfur-to-nitrogen ratio, accumulation of the β-subunit of β-conglycinin, a sulfur-poor seed storage protein of soybean (Glycine max [L.] Merr.), is elevated, whereas that of glycinin, a sulfur-rich storage protein, is reduced. Using transgenic Arabidopsis thaliana [L.] Heynh., it was found that the promoter from the gene encoding the β-subunit of β-conglycinin up-regulates gene expression under sulfur deficiency and down-regulates gene expression under nitrogen deficiency. To obtain an insight into the metabolic control of this regulation, the concentrations of metabolites related to the sulfur assimilation pathway were determined. Among the metabolites, O-acetyl-l-serine (OAS), one of the precursors of cysteine biosynthesis, accumulated to higher levels under low-sulfur and high-nitrogen conditions in siliques of transgenic A. thaliana. The pattern of OAS accumulation in response to various levels of sulfur and nitrogen was similar to that of gene expression driven by the β-subunit promoter. Elevated levels of OAS accumulation were also observed in soybean cotyledons cultured under sulfur deficiency. Moreover, OAS applied to in-vitro cultures of immature soybean cotyledons under normal sulfate conditions resulted in a high accumulation of the β-subunit mRNA and protein, whereas the accumulation of glycinin was reduced. These changes were very similar to the responses observed under conditions of sulfur deficiency. Our results suggest that the level of free OAS mediates sulfur- and nitrogen-regulation of soybean seed storage-protein composition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050634
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  • 6
    Electronic Resource
    Electronic Resource
    Electroporated protoplasts express seed specific gene promoters (1991)
    Springer
    Plant cell reports 9 (1991), S. 602-606 
    Details
    ISSN: 1432-203X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The soybean 7S seed storage protein, β-conglycinin, is comprised of three major subunits, α′, α, and β. Chimeric genes having β-conglycinin α′ and β subunit promoters and the β-glucuronidase gene coding sequence were constructed and electroporated into protoplasts prepared from three cultured cell lines and from tobacco mesophyll cells. The β-conglycinin promoters were active in all protoplasts examined, and their activities were 10–60% of that of the cauliflower mosaic virus 35S promoter. In electroporated protoplasts isolated from tobacco suspension cultures the time course of expression and the pattern of cell cycle dependency of the β-conglycinin promoters were similar to those of the 35S promoter. The responses to exogenously added L-methionine and abscisic acid, which are known to have differential effects on the expression of β-conglycinin promoters in cultured soybean cotyledons, were essentially the same among the promoters used. The results indicate that β-conglycinin promoters are expressed in electroporated protoplasts, but their regulation is relaxed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00231797
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  • 7
    Electronic Resource
    Electronic Resource
    Detection and characterization of nitrogen circulation through the sieve tubes and xylem vessels of rice plants (1997)
    Springer
    Plant and soil 196 (1997), S. 233-237 
    Details
    ISSN: 1573-5036
    Keywords: nitrogen ; 13N ; 15N ; phloem sap ; positron-emitting tracer imaging system ; rice ; xylem
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Nitrogen movement through the xylem vessels and sieve tubes in rice plants was studied using xylem and phloem sap analysis in combination with stable and radioactive nitrogen isotope techniques. More than 90% of nitrogen was translocated in the sieve tubes of rice plants as amino acids. When 15N (99.6 atom%) was applied as a nitrate to the root, 15N first appeared in phloem sap of the leaf sheath within 10 minutes and increased to 37 atom% excess 5 hours after the experiment had started. In long-term experiments, 63% of nitrogen in the phloem sap of the leaf sheath and 15% in that of the uppermost internode came from nitrogen absorbed within the last 24 hours and 50 hours, respectively. To obtain information about the more rapid circulation of nitrogen in the plant, radioactive 13N was used as a tracer. A positron-emitting tracer imaging system was used to show that 13N was transferred to the leaf sheath within 8 minutes of its application to the roots. Analysis of the xylem sap of the leaf sheath showed that when the nitrate was applied to the roots, most of the nitrogen in the xylem was transported as a nitrate. These data showed that phloem and xylem sap analysis together with the stable and radioactive nitrogen techniques provide a good method for the detection of nitrogen cycles in plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1004254124898
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  • 8
    Electronic Resource
    Electronic Resource
    Migration of heavy metals in two Japanese soils (1982)
    Springer
    Plant and soil 66 (1982), S. 299-316 
    Details
    ISSN: 1573-5036
    Keywords: Bio-toxic ; Cadmium ; Contamination ; Copper ; Copper ; Health hazard ; Heavy metals ; Lead ; Localisation ; Migration ; Nickel ; Pollution ; Zinc
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary The migration of common bio-toxic heavy metals in two typical soils of Japan under the influence of various leaching solutions was investigated. The results of the present study have indicated that the Pb and Cu ions were less mobile than those on Zn and Cd. Thus, the former two ions have largely been concentrated in the surface horizon while the latter two have been localised in the sub-surface layers. Ni has exhibited greater mobility than other heavy metals under all the leaching stress in both the soils. It is clear from the present study that Ni, Cd and Zn might pose a greater threat of ground water pollution than Cu and Pb. The specific migration properties of each metal ion varied depending on the nature of the ion and leaching solutions. The major soil factors governing the mobility of heavy metals in the soils have been discussed in the light of the results of the present investigation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02183797
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  • 9
    Electronic Resource
    Electronic Resource
    A dioxygenase gene (Ids2) expressed under iron deficiency conditions in the roots of Hordeum vulgare (1994)
    Springer
    Plant molecular biology 25 (1994), S. 705-719 
    Details
    ISSN: 1573-5028
    Keywords: chlorosis ; DNA sequence ; Ids2 ; iron deficiency ; MAs ; phytosiderophores
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A λzapII cDNA library was constructed from mRNA isolated from Fe-deficient barley roots and screened with cDNA probes made from mRNA of Fe-deficient and Fe-sufficient (control) barley roots. Seven clones were selected. Among them a clone having the putative full-length mRNA of dioxygenase as judged by northern hybridization was selected and named Ids2 (iron deficiency-specific clone 2). Using a cDNA fragment as probe, two clones from the genomic library (λEMBL-III) were isolated and one was sequenced. The predicted amino acid sequence of Ids2 resembled that of 2-oxoglutarate-dependent dioxygenase. Ids2 is expressed in the Fe-deficient barley roots but is not in the leaves. The expression is repressed by the availability of Fe. Ids2 was also strongly expressed under Mn deficiency and weakly under Zn deficiency or excess NaCl (0.5%). The upstream 5′-flanking region of Ids2 has a root-specific cis element of the CaMV 35S promoter and a nodule-specific element of leghemoglobin, a metal regulatory element (MRE) and several Cu regulatory elements (UAS) of yeast metallothionein (CUP1).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00029608
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  • 10
    Electronic Resource
    Electronic Resource
    Purification and characterization of nicotianamine synthase from Fe-deficient barley roots (1994)
    Springer
    Plant and soil 165 (1994), S. 173-179 
    Details
    ISSN: 1573-5036
    Keywords: barley roots ; Fe-deficiency ; mugineic acid ; nicotianamine synthase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Nicotianamine (NA), the key precursor of the mugineic acid family phytosiderophores (MAs), is synthesized from S-adenosylmethionine (SAM). The NA synthase was strongly induced by Fe-deficiency treatment, and the activity increased to the maximum level faster than the time of maximum level of MAs secretion and also before the appearance of severest chlorosis. The enzyme was mainly localized in the roots of barley. NA synthase had the optimum pH at 9.0, a molecular weight of about 40,000∼50,000 estimated by gel filtration or about 30,000 by SDS-PAGE. Using hydrophobic chromatography, hydroxylapatite chromatography, and preparative SDS-PAGE, NA synthase was purified as one band on SDS-PAGE.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00008059
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