Reciprocal regulation of the autophosphorylation of enzyme <scp>I<sup>Ntr</sup></scp> by glutamine and α‐ketoglutarate in <i><scp>E</scp>scherichia coli</i>

Lee, Chang-Ro; Park, Young-Ha; Kim, Miri; Kim, Yeon-Ran; Park, Soyoung; Peterkofsky, Alan; Seok, Yeong‐Jae

doi:10.1111/mmi.12196

Cited by 55 publications

(59 citation statements)

References 52 publications

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“…Using an in vitro-reconstituted system, they demonstrated that 2-OG and glutamine (signals of the carbon and nitrogen statuses) reciprocally regulate the phosphorylation state of PTS Ntr . Glutamine inhibits EI Ntr autophosphorylation, whereas 2-OG stimulates it, which is consistent with the accumulation of unphosphorylated EIIA Ntr under ammonium-sufficient conditions in vivo (124). The binding sites for glutamine and 2-OG were mapped to the GAF domain of EI Ntr (124).…”

Section: The Regulatory Pts (Pts Ntr )supporting

confidence: 65%

“…Glutamine inhibits EI Ntr autophosphorylation, whereas 2-OG stimulates it, which is consistent with the accumulation of unphosphorylated EIIA Ntr under ammonium-sufficient conditions in vivo (124). The binding sites for glutamine and 2-OG were mapped to the GAF domain of EI Ntr (124). However, glutamine, not 2-OG, was found to bind the GAF domain of EI Ntr from Sinorhizobium meliloti (125).…”

Section: The Regulatory Pts (Pts Ntr )supporting

confidence: 62%

“…The P II signal transduction proteins provide fail-safe integration of the carbon and nitrogen statuses through directly sensing the 2-OG concentration and also by sensing glutamine, either directly through the Q linker or indirectly via posttranslational modifications. Another well-suited module for integrating the carbon and nitrogen statuses is the E. coli PTS Ntr , as its phosphorelay cascade is modulated by both 2-OG and glutamine (124). However, despite several reported functions of PTS Ntr in different model bacteria, a direct connection between PTS Ntr and regulation of a specific metabolic pathway remains elusive.…”

Section: Discussionmentioning

confidence: 99%

“…Although the studies described above point to a possible role for 2-OG in communicating the carbon status to the PTS Ntr , the observation that glutamine binds to the GAF domain of EI Ntr suggests that this system is responsive to the nitrogen status (124,125). In the following paragraph, we discuss a potential hypothesis in which the PTS Ntr may signal nitrogen availability via regulation of potassium transport.…”

Section: The Regulatory Pts (Pts Ntr )mentioning

confidence: 91%

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The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite

Huergo

Dixon

2015

Microbiol Mol Biol Rev

242

221

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SUMMARYThe metabolite 2-oxoglutarate (also known as α-ketoglutarate, 2-ketoglutaric acid, or oxoglutaric acid) lies at the intersection between the carbon and nitrogen metabolic pathways. This compound is a key intermediate of one of the most fundamental biochemical pathways in carbon metabolism, the tricarboxylic acid (TCA) cycle. In addition, 2-oxoglutarate also acts as the major carbon skeleton for nitrogen-assimilatory reactions. Experimental data support the conclusion that intracellular levels of 2-oxoglutarate fluctuate according to nitrogen and carbon availability. This review summarizes how nature has capitalized on the ability of 2-oxoglutarate to reflect cellular nutritional status through evolution of a variety of 2-oxoglutarate-sensing regulatory proteins. The number of metabolic pathways known to be regulated by 2-oxoglutarate levels has increased significantly in recent years. The signaling properties of 2-oxoglutarate are highlighted by the fact that this metabolite regulates the synthesis of the well-established master signaling molecule, cyclic AMP (cAMP), inEscherichia coli.

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Section: The Regulatory Pts (Pts Ntr )supporting

confidence: 65%

Section: The Regulatory Pts (Pts Ntr )supporting

confidence: 62%

Section: Discussionmentioning

confidence: 99%

Section: The Regulatory Pts (Pts Ntr )mentioning

confidence: 91%

See 2 more Smart Citations

The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite

Huergo

Dixon

2015

Microbiol Mol Biol Rev

242

221

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“…Nevertheless, in bacteria also possessing EI, HPr, and sugar-specific EIIB and EIIC components, such as most Enterobacteriaceae, a cross talk between the two types of PTS exists (114,115). The activity of EI Ntr was recently shown to be antagonistically regulated by the metabolic intermediates situated at the intersection between carbon and nitrogen metabolism, namely, ␣-ketoglutarate and glutamine (116). Components of the PTS Ntr are found not only in Enterobacteriaceae but also in many proteobacteria that are devoid of any known EIIB and EIIC components.…”

Section: Fig 5 Pts-catalyzed Glucose Uptake and The Eiiamentioning

confidence: 99%

The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions

Deutscher

Aké

Derkaoui

et al. 2014

Microbiol Mol Biol Rev

342

374

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SUMMARY The bacterial phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS) carries out both catalytic and regulatory functions. It catalyzes the transport and phosphorylation of a variety of sugars and sugar derivatives but also carries out numerous regulatory functions related to carbon, nitrogen, and phosphate metabolism, to chemotaxis, to potassium transport, and to the virulence of certain pathogens. For these different regulatory processes, the signal is provided by the phosphorylation state of the PTS components, which varies according to the availability of PTS substrates and the metabolic state of the cell. PEP acts as phosphoryl donor for enzyme I (EI), which, together with HPr and one of several EIIA and EIIB pairs, forms a phosphorylation cascade which allows phosphorylation of the cognate carbohydrate bound to the membrane-spanning EIIC. HPr of firmicutes and numerous proteobacteria is also phosphorylated in an ATP-dependent reaction catalyzed by the bifunctional HPr kinase/phosphorylase. PTS-mediated regulatory mechanisms are based either on direct phosphorylation of the target protein or on phosphorylation-dependent interactions. For regulation by PTS-mediated phosphorylation, the target proteins either acquired a PTS domain by fusing it to their N or C termini or integrated a specific, conserved PTS regulation domain (PRD) or, alternatively, developed their own specific sites for PTS-mediated phosphorylation. Protein-protein interactions can occur with either phosphorylated or unphosphorylated PTS components and can either stimulate or inhibit the function of the target proteins. This large variety of signal transduction mechanisms allows the PTS to regulate numerous proteins and to form a vast regulatory network responding to the phosphorylation state of various PTS components.

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Metabolic Regulation and Coordination of the Metabolism in Bacteria in Response to a Variety of Growth Conditions

Shimizu

2015

Advances in Biochemical Engineering/Biotechnology

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Living organisms have sophisticated but well-organized regulation system. It is important to understand the metabolic regulation mechanisms in relation to growth environment for the efficient design of cell factories for biofuels and biochemicals production. Here, an overview is given for carbon catabolite regulation, nitrogen regulation, ion, sulfur, and phosphate regulations, stringent response under nutrient starvation as well as oxidative stress regulation, redox state regulation, acid-shock, heat- and cold-shock regulations, solvent stress regulation, osmoregulation, and biofilm formation, and quorum sensing focusing on Escherichia coli metabolism and others. The coordinated regulation mechanisms are of particular interest in getting insight into the principle which governs the cell metabolism. The metabolism is controlled by both enzyme-level regulation and transcriptional regulation via transcription factors such as cAMP-Crp, Cra, Csr, Fis, P(II)(GlnB), NtrBC, CysB, PhoR/B, SoxR/S, Fur, MarR, ArcA/B, Fnr, NarX/L, RpoS, and (p)ppGpp for stringent response, where the timescales for enzyme-level and gene-level regulations are different. Moreover, multiple regulations are coordinated by the intracellular metabolites, where fructose 1,6-bisphosphate (FBP), phosphoenolpyruvate (PEP), and acetyl-CoA (AcCoA) play important roles for enzyme-level regulation as well as transcriptional control, while α-ketoacids such as α-ketoglutaric acid (αKG), pyruvate (PYR), and oxaloacetate (OAA) play important roles for the coordinated regulation between carbon source uptake rate and other nutrient uptake rate such as nitrogen or sulfur uptake rate by modulation of cAMP via Cya.

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Reciprocal regulation of the autophosphorylation of enzyme I^Ntr by glutamine and α‐ketoglutarate in Escherichia coli

Cited by 55 publications

References 52 publications

The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite

The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite

The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions

Metabolic Regulation and Coordination of the Metabolism in Bacteria in Response to a Variety of Growth Conditions

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Reciprocal regulation of the autophosphorylation of enzyme INtr by glutamine and α‐ketoglutarate in Escherichia coli

Cited by 55 publications

References 52 publications

The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite

The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite

The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions

Metabolic Regulation and Coordination of the Metabolism in Bacteria in Response to a Variety of Growth Conditions

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Reciprocal regulation of the autophosphorylation of enzyme I^Ntr by glutamine and α‐ketoglutarate in Escherichia coli