Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 98 (1996), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Nitrate reductase (NR) activity is modulated in vivo by phosphorylation (inactivation)/dephosphorylation (activation) in response to light/dark signals. The dephosphorylation of phospho-NR in vitro, catalyzed by endogenous protein phosphatases, is known to be stimulated by 5′-AMP suggesting that this metabolite may be an important regulator of the activity of NR, e.g. under anoxia. To determine whether 5′-AMP might be a regulatory metabolite in vivo, excised spinach (Spinacia oleracea) and pea (Pisum sativum) leaves were provided 5-aminoimidazole-4-carboxamide riboside (AICAR) via the transpiration stream, and the apparent phosphorylation status of NR was assessed by assay of activity in the presence of free Mg2+. NR was activated in darkened spinach leaves in a time- and concentration-dependent manner when leaves were fed AICAR; there was also an accumulation of nitrite in treated leaves in the dark. The activation by AICAR could be blocked by several type 2A protein phosphatase inhibitors (microcystin-LR, okadaic acid and cantharidin), and was not the result of a reduction of kinase activity by lack of ATP because cellular adenylates were unaffected. It was confirmed that AICAR-P, but not AICAR, mimicked 5′-AMP in the activation of phospho-NR in vitro. Our results are consistent with the notion that AICAR is converted to the monophosphorylated derivative, which accumulates in cells and acts as a structural analog of 5′-AMP. Our results suggest that a rise in cytosolic [5′-AMP] may be sufficient to activate NR in vivo. AICAR should be a useful compound for identifying AMP-regulated processes in plant systems.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Studies were conducted to compare the modulation of β-nicotinamide adenine dinucleotide (NADH): nitrate reductase (NR; EC 1.6.6.1) and sucrose-phosphate synthase (SPS: EC 2.4.1.14) with respect to regulation by the inorganic anions, phosphate (P1), sulfate and tungstate. Following inactivation of both enzymes in vivo by transferring spinach plants (Spinacia oleracea L. cv. Bloomsdale) to a darkened growth chamber, spontaneous reactivation occurred in vitro when desalted leaf extracts were preincubated at 25°C prior to assay. All three inorganic anions inhibited SPS activation in vitro and also reduced the light activation of SPS in situ when they were fed to excised leaves via the transpiration stream. As expected, feeding tungstate to excised leaves prevented the light-dependent increase in extractable NR activity. However, in contrast to SPS, the light activation of NR in situ was relatively unaffected by Pi, and sulfate, and in vitro, both anions stimulated (rather than inhibited) the reactivation of NR. Part of the stimulation by Pi and sulfate was the result of increased ionic strength, and stimulation could also be demonstrated with other inorganic and organic salts. In the presence of high ionic strength (0.1 to 0.2 M KCl) the rate of NR activation in vitro was relatively constant when the pH of the preincubation medium was varied from pH 6.5 to 8.0, whereas in the absence of added salt the rate of activation was nearly zero at pH 6.5 but increased progressively as pH was raised. The stimulation by salts could be reversed, in part, by glycerol and ethylene glycol suggesting that hydrophobic interactions might play some role in the activation of NR.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 71 (1987), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Under drought, CO2 assimilation rates decrease already at small leaf water deficits. At least part of the inhibition is attributed to non-stomata1 effects at the chloroplast level, with electron transport and phosphorylation being main targets of inhibition. These findings are questioned by direct measurements of photosynthetic capacity with systems that are not Limited by stomata, e.g. leaf slices in solution or leaves at ex-ternal CO2 concentrations exceeding 5%. Here, photosynthesis was rather insensitive to dehydration down to 50–70% relative water content, and different plant species re-sponded in a very similar way. More severe dehydration affected not only pboto-synthesis, but also dark CO2 fixation and presumably also photorespiration. Rever-sible and unspecific inhibition is thought to be mediated mainly by increased concen-trations of solutes in dehydrated cells. Inhibition of photorespiration might favour photoinhibition when long-term water stress is coupled with full sunlight. Photo-inhibition, together with general senescence phenomena might be involved in long-term effects of water stress under natural drought conditions. This offers an explanation for the conflicting results of short-term water stress experiments and studies carried out under field conditions.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 111 (2001), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Feeding 5-aminoimidazole-4-carboxiamide ribonucleoside (AICAR) through the petiole of detached young barley leaves rapidly increased activities of NADH-nitrate reductase (NR) and glutamine synthetase (GS) in leaf extracts and at least partly prevented the usual slow decrease of these enzyme activities during prolonged illumination. Further, AICAR caused drastic changes in amino acid levels: glutamine and serine levels were increased whereas glutamate and glycine were decreased, probably indicating a higher GS activity and more rapid conversion of glycine into serine. The latter may be responsible for the higher ammonium contents found in AICAR treated leaves. We tentatively suggest that GS (located in the chloroplast) and glycine decarboxylase (located in the mitochondria) are regulated in a manner similar to NR. This is discussed in the light of recent reports that 14-3-3 isoforms exist in chloroplasts and that GS binds to 14-3-3s in vitro.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 5
    ISSN: 1432-2048
    Keywords: Ammonia ; Cytosol (pH) ; C3 and C4 plants ; Dye (pH-indicating) ; Vacuole (pH)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Atmospheric ammonia (NH3) from various anthropogenic sources has become a serious problem for natural vegetation. Ammonia not only causes changes in plant nitrogen metabolism, but also affects the acid-base balance of plants. Using the pH-sensitive fluorescent dyes pyranine and esculin, cytosolic and vacuolar pH changes were measured in leaves of C3 and C4 plants exposed for brief periods to concentrations of NH3 in air ranging from 1.33 to 8.29 μmol NH3 · mol-1 gas (0.94–5.86 mg · m-3). After a lag phase, uptake of NH3 from air at a rate of 200 nmol NH3 · m - 2 leaf area · s- 1 into leaves of Zea mays L. increased pyranine fluorescence indicating cytosolic alkalinisation. The increase was much larger in the dark than in the light. In illuminated leaves of the C3 plant Pelargonium zonale L. and the C4 plants Z. mays and Amaranthus caudatus L., NH3-dependent cytosolic alkalinisation was particularly pronounced when CO2 was supplied at very low levels (16 or 20 μmol CO2 · mol- 1 gas, containing 210 mmol O2 · mol- 1 gas). An increase in esculin fluorescence, which was smaller than that of pyranine, was indicative of trapping of some of the NH3 in the vacuoles of leaves of Spinacia oleracea L. and Z. mays. Photosynthesis and transpiration remained unchanged during exposure of illuminated leaves to NH3, yielding an influx of 200 nmol NH3 · m-2 leaf area · s-1 for up to 30 min, the longest exposure time used. Both CO2 and O2 influenced the extent of cytosolic alkalinisation. At 500 μmol CO2 · mol-1 gas the cytosolic alkalinisation was suppressed more than at 16 or 20 μmol CO2 · mol-1 gas. The suppressing effect of CO2 on the NH3induced alkalinisation was larger in illuminated leaves of the C4 plants Z. mays and A. caudatus than in leaves of the C3 plant P. zonale. A reduction of the O2 concentration from 210 to 10 mmol O2 · mol -1 gas, which inhibits photorespiration, increased the NH3induced cytosolic alkalinisation in C3 plants. Suppression by CO2 or O2 of the alkaline pH shift caused by the dissolution and protonation of NH3 in queous leaf compartments, and possibly by the production of organic compounds synthesised from atmospheric NH3, indicates that NH3 which enters leaves is rapidly assimilated if photosynthesis or photorespiration provide nitrogen acceptor molecules.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Planta 151 (1981), S. 375-380 
    ISSN: 1432-2048
    Keywords: Chloroplast volume ; Photosynthesis and chloroplast volume ; Spinacia ; Water stress
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. Isolated intact spinach chloroplasts respond to changes of the sorbitol concentration of the suspending medium as near-perfect osmometers within a large range of osmotic potentials. Under isotonic conditions (π=9–10 bar), their average osmotic volume is 24 μm3 and the total volume 36 μm3. The osmotic volume can be increased to 63 μm3 by lowering the sorbitol concentration until a critical osmotic potential of π=4 bar is reached. Below that value chloroplasts rupture. Between 10 bar and 4 bar, volume changes are reversible. 2. Increasing the chloroplast volume above 24 μm3 causes inhibition of photosynthesis, with 50% inhibition occurring at an osmotic potential of π=5–6 bar. This corresponds to an osmotic volume of 45–55 μm3. Depending on the duration of hypotonic treatment, inhibition of photosynthesis is more or less reversible. 3. Between 4 and 10 bar, the chloroplast envelope exhibits a very low permeability for ferricyanide, many metabolites, and soluble stroma proteins. 4. Electron transport is not inhibited by swelling of chloroplasts. Also, the ATP/ADP-ratio remains unchanged. 5. The solute concentration in the chloroplasts appears to be optimal for photosynthesis at 10 bar. Increasing the chloroplast volume causes inhibition of photosynthesis by dilution effects.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 7
    ISSN: 1432-2048
    Keywords: Cations and photosynthesis ; Chloroplast (low-salt effects) ; Light activation (photosynthesis enzymes) ; Photosynthesis ; Spinacia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The role of monovalent cations in the photosynthesis of isolated intact spinach chloroplasts was investigated. When intact chloroplasts were assayed in a medium containing only low concentrations of mono- and divalent cations (about 3 mval l-1), CO2-fixation was strongly inhibited although the intactness of chloroplasts remained unchanged. Addition of K+, Rb+, or Na+ (50–100 mM) fully restored photosynthesis. Both the degree of inhibition and restoration varied with the plant material and the storage time of the chloroplasts in “low-salt” medium. In most experiments the various monovalent cations showed a different effectiveness in restoring photosynthesis of low-salt chloroplasts (K+〉Rb+〉Na+). Of the divalent cations tested, Mg2+ also restored photosynthesis, but to a lesser extent than the monovalent cations. In contrast to CO2-fixation, reduction of 3-phosphoglycerate was not ihibited under low-salt conditions. In the dark, CO2-fixation of lysed chloroplasts supplied with ATP, NADPH, and 3-phosphoglycerate strictly required the presence of Mg2+ but was independent of monovalent cations. This finding excludes a direct inactivation of Calvin cycle enzymes as a possible basis for the inhibition of photosynthesis under low-salt conditions. Light-induced alkalization of the stroma and an increase in the concentration of freely exchangeable Mg2+ in the stroma, which can be observed in normal chloroplasts, did not occur under low-salt conditions but were strongly enhanced after addition of monovalent cations (50–100 mM) or Mg2+ (20–50 mM). The relevance of a light-triggered K+/H+ exchange at the chloroplast envelope is discussed with regard to the light-induced increase in the pH and the Mg2+ concentration in the stroma, which are thought to be obligatory for light activation of Calvincycle enzymes.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Planta 153 (1981), S. 430-435 
    ISSN: 1432-2048
    Keywords: Chloroplast ; Photosynthesis (stress recovery) ; Protoplast ; Spinacia ; Water stress
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The reversibility of the inhibition of photosynthetic reactions by water stress was examined with four systems of increasing complexity—stromal enzymes, intact chloroplasts, mesophyll protoplasts, and leaf slices. The inhibition of soluble chloroplast enzymes by high solute concentrations was instantly relieved when solutes were properly diluted. In contrast, photosynthesis was not restored but actually more inhibited when isolated chloroplasts exposed to hypertonic stress were transferred to conditions optimal for photosynthesis of unstressed chloroplasts. Upon transfer, chloroplast volumes increased beyond the volumes of unstressed chloroplasts, and partial envelope rupture occurred. In protoplasts and leaf slices, considerable and rapid, but incomplete restoration of photosynthesis was observed during transfer from hypertonic to isotonic conditions. Chloroplast envelopes did not rupture in situ during water uptake. It is concluded that inhibition of photosynthesis by severe water stress is at the biochemical level brought about in part by reversible inhibition of chloroplast enzymes and in part by membrane damage which requires repair mechanisms for reversibility. Both soluble enzymes and membranes appear to be affected by the increased concentration of internal solutes, which is caused by dehydration.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 9
    ISSN: 1432-2048
    Keywords: Adenine nucleotides (AMP, ATP) ; Light (enzyme modulation) ; Nitrate reductase ; Spinacia (nitrate reductase)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Nitrate reductase (NR; EC 1.6.6.1) in spinach (Spinacia oleracea L. cv. Polka F1) leaves showed reversible modulation, being activated in the light and inactivated in the dark (t/2 = 20–30 min). The large changes in enzyme activity during light-dark transients were observed only when assayed in buffers containing free Mg2+. In the presence of EDTA (5 mM), the enzyme activity was high and the light modulation was barely evident. The inactivation of NR in the dark could be totally prevented by anaerobiosis, or by feeding mannose or 2,4-dinitrophenol through the leaf petiole. All these treatments drastically decreased ATP levels and increased AMP levels in leaf extracts, thus pointing to a close correlation between adenine-nucleotide levels and NR activity. Treatment of leaves in the dark with 2,4-dinitrophenol or with anaerobiosis brought about an accumulation of nitrite, thus confirming that under these conditions NR remained active also in vivo. The in-vivo dark-inactivated enzyme was reactivated in vitro by preincubating a leaf extract with AMP in the presence of the myokinase inhibitor p1,p5-di(adenosine 5′)pentaphosphate. It is suggested that NR responds to artificially induced drastic changes in cytosolic adeninenucleotide levels, being active when ATP is low and AMP is high. Adenine nucleotides also appear to participate in the light-dark modulation of NR, but additional regulatory factors have to be postulated.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 10
    ISSN: 1432-2048
    Keywords: Inhibitor protein ; Nitrate reductase ; Protein phosphorylation ; Protein kinase ; Spinacia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The function of two proteins (P67 and P100) required for the MgATP-dependent inactivation of nitrate reductase (NR) from spinach leaves (Spinacia oleracea L.) was studied. When NR was incubated with γ-[32P]ATP and P67, NR-protein was phosphorylated, but without a change in NR activity. Protein P100 by itself was neither able to phosphorylate nor to inactivate NR, and when added together with P67 it did not change the extent of NR phosphorylation. However, when NR was first phosphorylated with MgATP and P67, subsequent addition of P100 after removal of unreacted ATP caused an immediate NR inactivation. In presence of both P67 and P100 the time-course of ATP-dependent NR phosphorylation paralleled the time course of inactivation. The extent of NR phosphorylation and of NR inactivation (in the presence of P67 plus P100) was similarly affected by metabolites or high salt concentrations. Magnesium (Mg2+) played a dual role in the inactivation process: the phosphorylation of NR by P67 was strictly Mg2+-dependent. Further, phospho-NR (+P100) was inactive only in the presence of Mg2+, but active in the presence of excess EDTA. Dephospho-NR appeared to be Mg2+-insensitive. The observations suggest that phosphorylation of NR by P67 is obligatory, but not sufficient for inactivation. In addition to protein phosphorylation, inactivation requires “binding” of an inhibitor protein (P100) to phospho-NR.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...