Coregulation of oxidized nicotinamide adenine dinucleotide (phosphate) transhydrogenase and glutamate dehydrogenase activities in enteric bacteria during nitrogen limitation

Liang, Amy; Houghton, Raymond L.

doi:10.1128/jb.146.3.997-1002.1981

Cited by 16 publications

(5 citation statements)

References 21 publications

(13 reference statements)

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“…These results contribute to clarify the controversy on GDH regulation by N-availability. In some cases GDH activity was determined in cells grown in L-glutamine as N-limiting condition [8,9,11], whereas in others a low amount of NH R Cl or L-glutamate was used [2,7,10]. The molecular mechanism that avoids gdhA repression in cells grown in L-glutamine is still unknown.…”

Section: Discussionmentioning

confidence: 99%

Transcriptional repression of gdhA in Escherichia coli is mediated by the Nac protein

Camarena

1998

FEMS Microbiology Letters

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In this work we show that the nac gene from Escherichia coli is transcriptionally active, and that its expression is dependent on NRI (NtrC) and sigma-54. Northern blot experiments show a monocistronic nac-specific mRNA that is detected when wildtype cells are grown in nitrogen-limiting conditions. Our data also show that in nitrogen-limiting conditions Nac is involved in the transcriptional repression of the gdhA gene (encoding glutamate dehydrogenase) except when L-glutamine is used as the only nitrogen source. Moreover, the high level of GDH activity observed in a nac mutant strain is reduced when a wild-type nac gene is introduced under control of the lac promoter in N-limiting conditions, but not in L-glutamine or N-excess. These results suggest the existence of an additional mechanism responsible for overcoming repression by Nac. z 1998 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

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Section: Discussionmentioning

confidence: 99%

Transcriptional repression of gdhA in Escherichia coli is mediated by the Nac protein

Camarena

1998

FEMS Microbiology Letters

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“…Figure 18(b) shows the decreased expression of gdhA as C/N ratio increases. Liang and Houghton [ 197 ] investigated the effect of NH 4 Cl concentration on GDH and GS activities and showed the upregulations of GDH and transhydrogenase activities at lower NH 4 Cl concentration.…”

Section: Nitrogen Regulationmentioning

confidence: 99%

“…As it has been shown that Nac is involved in the transcriptional repression of gdhA gene under N-limitation [ 203 ], Nac seems to repress gdhA gene as shown in Figure 18 , where it shows that the transcript level of gdhA gene is lower, while gltB and D genes are higher under N-limitation as compared to C-limitation. NADPH is an important cofactor in GDH and (GS)-GOGAT activities and it has been reported that transhydrogenase plays some role in the regulation of these pathways [ 197 ]. Under N-limitation, the glutamate and glutamine synthetic pathways are expected to be repressed due to shortage of NH 3 for those reactions, and thus NADPH is less utilized, resulting in overproduction of NADPH.…”

Section: Nitrogen Regulationmentioning

confidence: 99%

Metabolic Regulation of a Bacterial Cell System with Emphasis onEscherichia coliMetabolism

Shimizu

2013

ISRN Biochemistry

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It is quite important to understand the overall metabolic regulation mechanism of bacterial cells such as Escherichia coli from both science (such as biochemistry) and engineering (such as metabolic engineering) points of view. Here, an attempt was made to clarify the overall metabolic regulation mechanism by focusing on the roles of global regulators which detect the culture or growth condition and manipulate a set of metabolic pathways by modulating the related gene expressions. For this, it was considered how the cell responds to a variety of culture environments such as carbon (catabolite regulation), nitrogen, and phosphate limitations, as well as the effects of oxygen level, pH (acid shock), temperature (heat shock), and nutrient starvation.

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“…These results contribute to clarify the controversy on GDH regulation by N‐availability. In some cases GDH activity was determined in cells grown in l ‐glutamine as N‐limiting condition [8, 9, 11], whereas in others a low amount of NH 4 Cl or l ‐glutamate was used [2, 7, 10]. The molecular mechanism that avoids gdhA repression in cells grown in l ‐glutamine is still unknown.…”

Section: Discussionmentioning

confidence: 99%

“…In contrast, the K. aerogenes hutC gene is only slightly regulated by nitrogen conditions in E. coli [6]. In addition, there are conflicting reports regarding GDH regulation by N‐availability [2, 7–11], making it difficult to conclude if histidase and GDH are regulated in E. coli .…”

Section: Introductionmentioning

confidence: 99%

Transcriptional repression ofgdhAinEscherichia coliis mediated by the Nac protein

Camarena

Poggio

Garcı́a

et al. 1998

FEMS Microbiology Letters

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In this work we show that the nac gene from Escherichia coli is transcriptionally active, and that its expression is dependent on NRI (NtrC) and sigma-54. Northern blot experiments show a monocistronic nac-specific mRNA that is detected when wild-type cells are grown in nitrogen-limiting conditions. Our data also show that in nitrogen-limiting conditions Nac is involved in the transcriptional repression of the gdhA gene (encoding glutamate dehydrogenase) except when L-glutamine is used as the only nitrogen source. Moreover, the high level of GDH activity observed in a nac mutant strain is reduced when a wild-type nac gene is introduced under control of the lac promoter in N-limiting conditions, but not in L-glutamine or N-excess. These results suggest the existence of an additional mechanism responsible for overcoming repression by Nac.

show abstract

Coregulation of oxidized nicotinamide adenine dinucleotide (phosphate) transhydrogenase and glutamate dehydrogenase activities in enteric bacteria during nitrogen limitation

Cited by 16 publications

References 21 publications

Transcriptional repression of gdhA in Escherichia coli is mediated by the Nac protein

Transcriptional repression of gdhA in Escherichia coli is mediated by the Nac protein

Metabolic Regulation of a Bacterial Cell System with Emphasis onEscherichia coliMetabolism

Transcriptional repression ofgdhAinEscherichia coliis mediated by the Nac protein

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