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  • 1
    Electronic Resource
    Electronic Resource
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 108 (2000), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Reproductive stages of 5 japonica, 9 indica, and 2 javanica cultivars of rice (Oryza sativa L.) were provided to compare the contents of protein for cytosolic glutamine synthetase (GS1; EC 6.3.1.2) in the lowest position of the attached leaf blade (position 6 from the primary leaf) and those for NADH-glutamate synthase (NADH-GOGAT; EC 1.4.1.14) in non-green portion of the expanding 10th leaf blade. Some of the indica cultivars, including Kasalath, contained GS1 protein twice as high as other japonica and javanica cultivars based on total leaf nitrogen. Most of the indica cultivars, on the other hand, contained less NADH-GOGAT protein than japonica and javanica cultivars. Immunostaining proved that GS1 protein was located in vascular tissues of the leaf blades of Kasalath, which was identical to our previous results with a japonica cultivar [Sakurai et al. (1996) Planta 200: 306–311]. Although relative contents of GS1 protein in the leaf blade of Kasalath increased as a function of leaf age, GS1 activity remained relatively constant. In addition, Kasalath showed lower activity than other japonica and javanica cultivars, especially during leaf expansion. GS1 activity, based on GS1 protein amount, changed during the life span of the leaf blade and we thus assume that GS1 activity was modulated post-translationally in rice leaves.
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  • 2
    Electronic Resource
    Electronic Resource
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 113 (2001), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In order to estimate whether cytosolic glutamine synthetase (GS1; EC 6.3.1.2) is partly coupled to the reaction of phenylalanine ammonia-lyase (PAL; EC 4.3.1.5) in developing organs of rice (Oryza sativa L.), we compared the expression pattern of transcripts and proteins for GS1 and PAL in the tissue sections from leaf blades at various stages of development. In immature vascular bundles of unexpanded leaf blades, GS1 mRNA was mainly detected in xylem parenchyma cells, mestome-sheath cells, and sclerenchyma cells. PAL transcripts were also accumulated in these cell types. Vascular bundles in midribs of immature leaf blades contained mRNAs and proteins for both GS1 and PAL abundantly in sclerenchyma cells, although distribution of these two proteins was not completely overlapped. In immature vascular bundles in midribs, lignin deposition was observed in cell walls of xylem parenchyma cells, mestome-sheath cells and sclerenchyma cells. These results implied that a part of GS1 in unexpanded leaf blades is possibly involved in reassimilation of ammonia released from PAL reaction during the lignin production.
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  • 3
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] To the editor: As concerned plant scientists at major plant science research institutions in Japan, we would like to express our collective concern over the impact of Japanese public resistance to plant genetic engineering on the actions of local and national government. We are concerned that ...
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 72 (1988), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Localization of two isoforms of glutamine synthetase (GS; EC 6.3.1.2) was investigated in different cell types, mesophyll cells and bundle sheath cells, of corn (Zea mays L. var. W64A × W182E) leaves by using ion exchange chrotnatography. In whole leaf extracts, relative activities of GS1 (cytosolic GS) and GS2 (chloroplastic GS) were almost equal. Purified mesophyll protoplasts and bundle sheath strands also showed similar proportions of GS1 and GS2. Methionine sulfoximine (1 mM) enhanced the accumulation of ammonia when mesophyll protoplasts were incubated with nitrite or when bundle sheath strands were incubated with glycine. This clearly indicates a spatial separation of metabolism of NH+4 derived from photorespiration and from reduction of NOJ.
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 74 (1988), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A carrot (Daucus carota L. cv. MS Yonsun) cell line previously selected to be tolerant to Al supply was re-evaluated by culturing with hardly soluble or ionic Al. When insoluble Al-phosphate (2.0 mM) was supplied as a sole source of phosphate at an initial pH of 5.6, the selected cell line, but not wild-type cells, grew normally corresponding to the growth of the cells supplied with Na-phosphate in the absence of Al Under these conditions, the selected cells excreted large amounts of citrate into the medium. Insoluble Fe-phosphate could also be utilized as a phosphate source by the selected cells. Excretion of citrate was, however, not detected when the cells were cultured in the absence of insoluble phosphate. The selected cells were less tolerant against soluble. Al ions than the wild-type cells.
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 70 (1987), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The photorespiratory nitrogen cycle was initially thought to be a closed cyclic process. If this were true the loss of glutamate, glutamine, serine or glycine to other processes, such as protein synthesis or export from the leaves, would not be possible in a stoichiometric sense. However, recent studies with [15N]-labeled amino acids show that there are alternative sources of nitrogen for photorespiration, indicating that the nitrogen cycle is not a closed cyclic system. In addition recent work with 15NH4Cl and [15N]-glycine and a metabolically competent mitochondria system has shown that glutamate is synthesized in the mitochondria. Hence the glutamate dehydrogenase (GDH, EC 1.4.1.2) in mitochondria could also be active in the reassimilation of NH4. We would like to propose that one function of mitochondrial GDH is to synthesize glutamate from some of the NH4 released by photorespiration and that this glutamate represents a reserve for use in biosynthetic reactions.
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  • 7
    ISSN: 1432-2048
    Keywords: Cellular localization ; NADH-glutamate synthase ; Nitrogen metabolism ; Oryza (glutamate synthase)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Tissue and cellular localization of NADH-dependent glutamate synthase (NADH-GOGAT, EC 1.4.1.14) in the unexpanced leaf blades and young grains of rice (Oryza sativa L.) was investigated using tissue-print immunoblot and immunocytological methods with an affinity-purified anti-NADH-GOGAT immunoglobulin G. Tissue-print immunoblots showed that the NADH-GOGAT protein was mostly located in large and small vascular bundles of the unexpanded blades. When the cross-sections (10μ in thickness) prepared from the paraffin-embedded blades were stained with the antibody, the NADH-GOGAT protein was detected in vascular-parenchyma cells and mestome-sheath cells. In developing grains, the NADH-GOGAT protein was detected in both phloem- and xylem-parenchyma cells of dorsal and lateral vascular bundles, and in the nucellar projection, nucellar epidermis, and aleurone cells. On the other hand, ferredoxin (Fd)-dependent GOGAT (EC 1.4.7.1) was located mainly in mesophyll cells of the leaf blade and in chloroplast-containing cross-cells of the pericarp of the grains. The spatial expression of these GOGAT proteins indicates distinct and non-overlapping roles in rice plants. In the leaf blades and young grains, NADH-GOGAT could be involved in the synthesis of glutamate from the glutamine that is transported through the vascular system from roots and senescing tissues.
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  • 8
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The mRNA and protein for NADH-dependent glutamate synthase (NADH-GOGAT; EC 1.4.1.14) in root tips of rice (Oryza sativa L. cv. Sasanishiki) plants increases dramatically within 12 h of supplying a␣low concentration (〉0.05 mM) of ammonium ions (T.␣Yamaya et al., 1995, Plant Cell Physiol 36: 1197–1204). To identify the specific cells which are responsible for this rapid increase, the cellular localization of NADH-GOGAT protein was investigated immunocytologically with an affinity-purified anti-NADH-GOGAT immunoglobulin G. When root tips (〉1 mm) of rice seedlings which had been grown for 26 d in water were immuno-stained, signals for the NADH-GOGAT protein were detected in the central cylinder, in the apical meristem, and in the primordia of the secondary roots. Signals for ferredoxin-dependent GOGAT (Fd-GOGAT; EC 1.4.7.1) protein were also seen in the same three areas. When the roots were supplied with 1 mM ammonium ions for 24 h, there were strong signals for the NADH-GOGAT protein in two cell layers of the root surface, i.e. epidermis and exodermis, in addition to the cells giving signals in the absence of ammonium ions. The supply of ammonium ions was less effective on the profile of signals for Fd-GOGAT. Although the supply of ammonium ions had less effect on the expression of cytosolic glutamine synthetase (GS; EC 6.3.1.2), this enzyme was also found to be located in the epidermis and exodermis, as well as in the central cylinder and cortex. The results indicate that NADH-GOGAT, coupled to the cytosolic GS reaction, is probably important for the assimilation of ammonium ions in the two cell layers of the root surface.
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  • 9
    ISSN: 1432-2048
    Keywords: Enzyme localization ; Glutamine synthetase ; Nitrogen remobilization ; Oryza ; Vascular bundle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cellular localization of cytosolic glutamine synthetase (GS1; EC 6.3.1.2) in vascular bundles of leaf blades of rice (Oryza sativa L.), at the stage at which leaf blades 6 (the lowest position) to 10 were fully expanded, was investigated immunocytologically with an affinity-purified anti-GS1 immunoglobulin G. Strong signals for GS1 protein were detected in companion cells of large vascular bundles when blades 6–8 were tested. Signals for GS1 were also observed in vascular-parenchyma cells of both large and small vascular bundles. The results further support our hypothesis that GS1 is important for the export of leaf nitrogen from senescing leaves. The signals in companion cells were less striking in the younger green leaves and were hardly detected in the non-green portion of the 11th blade. In the non-green blades, strong signals for GS1 protein were detected in sclerenchyma and xylemparenchyma cells. When total GS extracts prepared from the 6th,10th, and the non-green 11th blades were subjected to anion-exchange chromatography, the activity of GS1 was clearly separated from that of chloroplastic GS, indicating that GS1 proteins detected in the vascular tissues were able to synthesize glutamine. The function of GS1 detected in the developing leaves is discussed.
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  • 10
    Publication Date: 2004-08-01
    Print ISSN: 1087-0156
    Electronic ISSN: 1546-1696
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Springer Nature
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