Nitrate Assimilation

Author(s):  
Niharika Shankar ◽  
H. S. Srivastava
Keyword(s):  
1993 ◽  
Vol 89 (1) ◽  
pp. 71-76
Author(s):  
Lucia Merlo ◽  
Massimo Ferretti ◽  
Rossella Ghisi ◽  
Calvino Passera

2016 ◽  
Vol 52 (92) ◽  
pp. 13511-13514 ◽  
Author(s):  
Zoë A. E. Waller ◽  
Benjamin J. Pinchbeck ◽  
Bhovina Seewoodharry Buguth ◽  
Timothy G. Meadows ◽  
David J. Richardson ◽  
...  

Ligand-specific control of nitrate assimilation inParacoccus denitrificansby stabilization of DNA G-quadruplex in the promoter region ofnas.


PLoS Genetics ◽  
2019 ◽  
Vol 15 (2) ◽  
pp. e1007986 ◽  
Author(s):  
Eduard Ocaña-Pallarès ◽  
Sebastián R. Najle ◽  
Claudio Scazzocchio ◽  
Iñaki Ruiz-Trillo

2014 ◽  
Vol 132 ◽  
pp. 391-412 ◽  
Author(s):  
K.L. Karsh ◽  
T.W. Trull ◽  
D.M. Sigman ◽  
P.A. Thompson ◽  
J. Granger

1998 ◽  
Vol 18 (3) ◽  
pp. 1339-1348 ◽  
Author(s):  
Joseph Strauss ◽  
M. Isabel Muro-Pastor ◽  
Claudio Scazzocchio

ABSTRACT The regulation of nitrate assimilation seems to follow the same pattern in all ascomycetes where this process has been studied. We show here by in vitro binding studies and a number of protection and interference techniques that the transcription factor mediating nitrate induction in Aspergillus nidulans, a protein containing a binuclear zinc cluster DNA binding domain, recognizes an asymmetrical sequence of the form CTCCGHGG. We further show that the protein binds to its consensus site as a dimer. We establish the role of the putative dimerization element by its ability to replace the analogous element of the cI protein of phage λ. Mutagenesis of crucial leucines of the dimerization element affect both the binding ability of the dimer and the conformation of the resulting protein-DNA complex. This is the first case to be described where a dimer recognizes such an asymmetrical nonrepeated sequence, presumably by each monomeric subunit making different contacts with different DNA half-sites.


1982 ◽  
Vol 38 (10) ◽  
pp. 1208-1210 ◽  
Author(s):  
M. H. Siddiqui ◽  
Anjali Mathur ◽  
S. N. Mathur

2018 ◽  
Vol 87 (2) ◽  
Author(s):  
Kimberly L. James ◽  
Austin B. Mogen ◽  
Jessica N. Brandwein ◽  
Silvia S. Orsini ◽  
Miranda J. Ridder ◽  
...  

ABSTRACTStaphylococcus aureusnitric oxide synthase (saNOS) is a major contributor to virulence, stress resistance, and physiology, yet the specific mechanism(s) by which saNOS intersects with other known regulatory circuits is largely unknown. The SrrAB two-component system, which modulates gene expression in response to the reduced state of respiratory menaquinones, is a positive regulator ofnosexpression. Several SrrAB-regulated genes were also previously shown to be induced in an aerobically respiringnosmutant, suggesting a potential interplay between saNOS and SrrAB. Therefore, a combination of genetic, molecular, and physiological approaches was employed to characterize anos srrABmutant, which had significant reductions in the maximum specific growth rate and oxygen consumption when cultured under conditions promoting aerobic respiration. Thenos srrABmutant secreted elevated lactate levels, correlating with the increased transcription of lactate dehydrogenases. Expression of nitrate and nitrite reductase genes was also significantly enhanced in thenos srrABdouble mutant, and its aerobic growth defect could be partially rescued with supplementation with nitrate, nitrite, or ammonia. Furthermore, elevated ornithine and citrulline levels and highly upregulated expression of arginine deiminase genes were observed in the double mutant. These data suggest that a dual deficiency in saNOS and SrrAB limitsS. aureusto fermentative metabolism, with a reliance on nitrate assimilation and the urea cycle to help fuel energy production. Thenos,srrAB, andnos srrABmutants showed comparable defects in endothelial intracellular survival, whereas thesrrABandnos srrABmutants were highly attenuated during murine sepsis, suggesting that SrrAB-mediated metabolic versatility is dominantin vivo.


2001 ◽  
Vol 32 (3) ◽  
pp. 187-194 ◽  
Author(s):  
Joaquim Albenísio Gomes da Silveira ◽  
Roberto Cezar Lobo da Costa ◽  
José Tadeu Abreu Oliveira

1981 ◽  
Vol 8 (6) ◽  
pp. 515 ◽  
Author(s):  
MS Naik ◽  
DJD Nicholas

In wheat leaf discs the evolution of 14CO2 from exogenously supplied 14C-labelled citric acid cycle intermediates was stimulated during the in situ anaerobic reduction of nitrate in the dark. Under these conditions, however, [1,4-14C]succinate was not metabolized. Similarly, when leaves were allowed to assimilate 14CO2 in the dark, thus producing endogenously labelled organic acids, the subsequent evolution of 14CO2 from discs prepared from these leaves was strongly dependent on nitrate reduction. A 1 : 1 stoichiometry between nitrite production and CO2 evolution was recorded during this in situ reduction of nitrate. The in situ reduction of nitrate was inhibited by malonate and D-malate and this effect was reversed by fumarate, probably by generating L-malate within the mitochondria. Mitochondrial NAD-malic enzyme (decarboxylating) (EC 1.1.1.38) was similarly inhibited competitively by malonate and D-malate, but not by succinate. These results indicate that the citric acid cycle dehydrogenases which generate CO2 supply NADH for nitrate reduction in wheat leaves. It is likely that, under anaerobic conditions, nitrate acts as an alternative oxidant to O2 for the NADH generated by the citric acid cycle dehydrogenases resulting in simultaneous evolution of CO2. This ensures that the citric acid cycle operates at the required rate for nitrate assimilation.


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