The Effect of Phosphinothricin on the Assimilation of Ammonia in Plants

1984 ◽  
Vol 39 (5) ◽  
pp. 500-504 ◽  
Author(s):  
Aloysius Wild ◽  
Remigius Manderscheid
Keyword(s):  
Glutamine Synthetase ◽  
Nitrogen Assimilation ◽  
Photosynthetic Activity ◽  
Light Period ◽  
Methionine Sulfoximine ◽  
Nitrogen Compounds ◽  
Strong Reduction ◽  
Strong Inhibitor ◽  
Ammonia Accumulation

The effects of ᴅʟ-phosphinothricin and L-methionine sulfoximine on the enzymes of nitrogen assimilation were studied. Furthermore we investigated the accumulation of ammonia and the photosynthetic activity after the treatment of mustard plants with phosphinothricin. Phosphino-thricin was a specific and very strong inhibitor of glutamine synthetase. Major differences, however, were found between the phosphinothricin affinity of the leaf enzyme and that of the root of mustard plants. The leaf enzyme was 50% inhibited at a concentration of 10-4 m phosphinothricin (pI50 = 4), whereas the root enzyme already showed the same effect at a concentration of 2 × 10-5m (pI50 = 4.7). In addition Ki values of about 0.03 mм for the leaf enzyme and 0.002 mм for the root enzyme respectively were determined. Phosphinothricin treatment of plants caused an ammonia accumulation in tissues. The accumulation was light dependent. At the beginning of the light period the major sources of ammonia accumulation could be the nitrogen assimilation as well as catabolic processes of nitrogen compounds. A clear contribution of photorespiration was only found when higher concentrations of ammonia were reached. The application of phosphinothricin induced a strong reduction of CO2 assimilation.

Effects of Methionine Sulfoximine and Glycine on Nitrogen Metabolism of Maize Leaves in the Light

1983 ◽  
Vol 10 (2) ◽  
pp. 187 ◽  
Author(s):  
MG Berger ◽  
HP Fock
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamine Synthetase ◽  
Nitrogen Cycling ◽  
Co2 Assimilation ◽  
Methionine Sulfoximine ◽  
Co2 Evolution ◽  
Ammonia Content ◽  
Ammonia Accumulation ◽  
Maize Leaves

Detached maize leaves with their cut bases in water or in solutions containing 15 mM [14C, 15N]glycine, 15 mM [14C]glutamate, 5 mM methionine sulfoximine (an inhibitor of glutamine synthetase) or the appropriate amino acid plus inhibitor, were incubated for up to 135 min in the light. The concentrations and the 15N content of ammonia and of amino acids involved in photorespiratory nitrogen cycling were determined. Incubation with methionine sulfoximine or glycine increased the ammonia content significantly, whereas glutamate showed no effect. The nitrogen of glycine was metabolized into serine and ammonia. Ammonia was first recycled into glutamine, and then into glutamate. The glycine carbon skeleton served as a precursor for serine. Based on the data for ammonia accumulation the minimum rate of photorespiratory CO2 evolution in maize leaves was estimated to be about 1% of the rate of CO2 assimilation.

Control of nitrogen assimilation in Stichococcus bacillaris by growth conditions

1987 ◽  
Vol 65 (3) ◽  
pp. 432-437 ◽  
Author(s):  
Iftikhar Ahmad ◽  
Johan A. Hellebust
Keyword(s):  
Glutamine Synthetase ◽  
Nitrogen Assimilation ◽  
Continuous Light ◽  
Synthetase Activity ◽  
Glutamine Synthetase Activity ◽  
Dark Cycle ◽  
Continuous Darkness ◽  
Cell Carbon ◽  
Stichococcus Bacillaris ◽  
Mixotrophic Conditions

Stichococcus bacillaris Naeg. (Chlorophyceae) grown on a 12 h light: 12 h dark cycle divides synchronously under photoautotrophic conditions and essentially nonsynchronously under mixotrophic conditions. Photoassimilation of carbon under photoautotrophic conditions was followed by a decline in cell carbon content during the dark period, whereas under mixotrophic conditions cell carbon increased throughout the light–dark cycle. The rates of nitrogen assimilation by cultures grown on either nitrate or ammonium declined sharply during the dark, and these declines were most pronounced under photoautotrophic conditions. Photoautotrophic cells synthesized glutamine synthetase and NADPH – glutamate dehydrogenase (GDH) exclusively in the light, whereas in mixotrophic cells about 20% of the total synthesis of these enzymes during one light–dark cycle occurred in the dark. NADH–GDH was synthesized almost continuously over the entire light–dark cycle. In the dark, both under photoautotrophic and mixotrophic conditions, the alga contained more than 50% of glutamine synthetase in an inactive form, which was reactivated in vitro in the presence of mercaptoethanol and in vivo after returning the cultures to the light. The thermal stability of glutamine synthetase activity was less in light-harvested cells than in dark-harvested cells. The inactivation of glutamine synthetase did not occur in cultures growing either heterotrophically in continuous darkness or photoautotrophically in continuous light. This enzyme appears to be under thiol control only in cells grown under alternating light–dark conditions, irrespective of whether this light regime results in synchronous cell division or not.

scholarly journals The sRNA NsiR4 is involved in nitrogen assimilation control in cyanobacteria by targeting glutamine synthetase inactivating factor IF7

2015 ◽  
Vol 112 (45) ◽  
pp. E6243-E6252 ◽  
Author(s):  
Stephan Klähn ◽  
Christoph Schaal ◽  
Jens Georg ◽  
Desirée Baumgartner ◽  
Gernot Knippen ◽  
...  
Keyword(s):  
Glutamine Synthetase ◽  
Nitrogen Metabolism ◽  
Nitrogen Assimilation ◽  
Nitrogen Sources ◽  
Transcriptome Profiling ◽  
Site Directed Mutagenesis ◽  
Reporter System ◽  
Available Nitrogen ◽  
Mrna Accumulation

Glutamine synthetase (GS), a key enzyme in biological nitrogen assimilation, is regulated in multiple ways in response to varying nitrogen sources and levels. Here we show a small regulatory RNA, NsiR4 (nitrogen stress-induced RNA 4), which plays an important role in the regulation of GS in cyanobacteria. NsiR4 expression in the unicellularSynechocystissp. PCC 6803 and in the filamentous, nitrogen-fixingAnabaenasp. PCC 7120 is stimulated through nitrogen limitation via NtcA, the global transcriptional regulator of genes involved in nitrogen metabolism. NsiR4 is widely conserved throughout the cyanobacterial phylum, suggesting a conserved function. In silico target prediction, transcriptome profiling on pulse overexpression, and site-directed mutagenesis experiments using a heterologous reporter system showed that NsiR4 interacts with the 5′UTR ofgifAmRNA, which encodes glutamine synthetase inactivating factor (IF)7. InSynechocystis, we observed an inverse relationship between the levels of NsiR4 and the accumulation of IF7 in vivo. This NsiR4-dependent modulation ofgifA(IF7) mRNA accumulation influenced the glutamine pool and thusNH4+assimilation via GS. As a second target, we identifiedssr1528, a hitherto uncharacterized nitrogen-regulated gene. Competition experiments between WT and an ΔnsiR4KO mutant showed that the lack of NsiR4 led to decreased acclimation capabilities ofSynechocystistoward oscillating nitrogen levels. These results suggest a role for NsiR4 in the regulation of nitrogen metabolism in cyanobacteria, especially for the adaptation to rapid changes in available nitrogen sources and concentrations. NsiR4 is, to our knowledge, the first identified bacterial sRNA regulating the primary assimilation of a macronutrient.

Studies on possible routes of ammonium assimilation in soybean root nodule bacteroids

1973 ◽  
Vol 19 (12) ◽  
pp. 1493-1499 ◽  
Author(s):  
Stanley D. Dunn ◽  
Robert V. Klucas
Keyword(s):  
Glutamine Synthetase ◽  
Nitrogen Assimilation ◽  
Reductive Amination ◽  
Root Nodule ◽  
Root Nodules ◽  
Ammonium Assimilation ◽  
Kinetic Properties ◽  
Transferase Activity ◽  
Soybean Root

Glutamine amide–2-oxoglutarate aminotransferase NAD+ oxidoreductase (GOGAT), glutamine synthetase (GS), glutamate dehydrogenase (GD), and alanine dehydrogenase (AD) were studied in soybean root nodules. GS, GOGAT, and AD were present in bacteroids at levels that could account for ammonium assimilation, but GD activity was quite low. The total activities of GS and GD were higher in the cytosol than in the bacteroids by factors of 20 and 7, respectively, whereas GOGAT was not detected in the cytosol. GS (transferase activity) was inhibited by alanine, CTP, glycine, and tryptophan at 5 mM but was relatively unaffected by asparagine, aspartic acid, CMP, glucosamine, and histidine at 5 mM. GOGAT activity was unaffected by ATP, ADP, 8-hydroxyquinoline, and 1,10-phenanthroline but was inhibited by EDTA, citrate, and parachloromercuribenzoate. GOGAT activity (reductive amination) was also inhibited 97% by preincubation with 10−4 M azaserine for 30 min but GD activity was inhibited only 13%. The apparent Km values for NH4+ by AD was 7.4 × 10−3 M and by GD was 7.3 × 10−2 M while for glutamine by GOGAT it was 9.3 × 10−5 M. Activities and kinetic properties for these enzymes may suggest potential routes of nitrogen assimilation in vivo.

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