Differential effects of exogenous L-glutamine, L-glutamic acid, sodium glutamate, and casamino acids on glutamine synthetase and nitrate reductase in isolated pea roots cultured with or without sucrose

1981 ◽  
Vol 59 (7) ◽  
pp. 1121-1127 ◽  
Author(s):  
J. Sahulka ◽  
L. Lisá

Exogenous L-glutamine, the sodium salt of L-glutamic acid, and casamino acids do not decrease glutamine synthetase (GS) level in isolated pea (Pisum sativum L. cv. Jupiter and cv. Proteus) roots cultured with 20 g∙L−1 sucrose while L-glutamic acid does decrease it. The effect of L-glutamic acid is stronger in solutions lacking nitrate. By contrast, only the exogenous sodium salt of L-glutamic acid does not enhance the decrease in GS level caused by sugar starvation in isolated roots cultured without any sugar while, the other compounds tested do enhance this decrease. These facts confirm our earlier conclusion that sugar availability and the concentration of H+ ions are more important for GS level regulation in pea roots than nitrogen substrate availability and the presence of the end products. Nitrate reductase (NR) level is depressed by exogenous L-glutamine, the sodium salt of L-glutamic acid, casamino acids, and a low (0.2 mM) concentration of L-glutamic acid whereas it is increased by higher (0.8 and 1.0 mM) concentrations of L-glutamic acid, by α-ketoglutaric acid (0.4 to 0.6 mM), and by nitric acid (0.2 to 0.4 mM) added to saturating concentration (10 mM) of nitrate present in the form of potassium and calcium salts. The negative effect of L-glutamine, sodium glutamate, and casamino acids can be reversed by L-glutamic acid. This suggests that more mechanisms may be involved in NR regulation by these compounds and that the mechanism controlled by increased concentration of H+ ions is of great importance.

2009 ◽  
Vol 191 (9) ◽  
pp. 3050-3058 ◽  
Author(s):  
Sadanobu Abe ◽  
Ayako Yasumura ◽  
Teruo Tanaka

ABSTRACT Expression of the gene for the extracellular alkaline protease (aprE) of Bacillus subtilis is subject to regulation by many positive and negative regulators. We have found that aprE expression was increased by disruption of the glutamine synthetase gene glnA. The increase in aprE expression was attributed to a decreased in expression of scoC, which encodes a negative regulator of aprE expression. The glnA effect on scoC expression was abolished by further disruption of tnrA, indicating that aprE expression is under global regulation through TnrA. In the scoC background, however, aprE expression was decreased by glnA deletion, and it was shown that the decrease was due to a defect in positive regulation by DegU. Among the genes that affect aprE expression through DegU, the expression of degR, encoding a protein that stabilizes phosphorylated DegU, was inhibited by glnA deletion. It was further shown that the decrease in degR expression by glnA deletion was caused by inhibition of the expression of sigD, encoding the σD factor, which is required for degR expression. In accordance with these findings, the expression levels of aprE-lacZ in glnA scoC degR and scoC degR strains were identical. These results led us to conclude that glnA deletion brings about two effects on aprE expression, i.e., a positive effect through inhibition of scoC expression and a negative effect through inhibition of degR expression, with the former predominating over the latter.


1960 ◽  
Vol 198 (2) ◽  
pp. 227-229 ◽  
Author(s):  
Leon Goldstein ◽  
J. H. Copenhaver

Injection of sodium glutamate had no significant effect on renal glutaminase I activity in untreated rats but suppressed the rise in enzyme activity which follows repeated ammonium chloride administration. Injection of glutamine produced a small rise in enzyme activity in untreated rats but suppressed the enzyme response in ammonium chloride-treated animals. Injection of glycine had no significant effect on enzyme activity in treated or untreated rats. A significant fall in renal glutamic acid concentration was observed 2 hours after the administration of ammonium chloride. These results suggest that there is a relation between the concentration of glutamic acid and the synthesis of glutaminase I in the kidney of the rat.


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