The phosphotransferase protein EIIA<sup>Ntr</sup> modulates the phosphate starvation response through interaction with histidine kinase PhoR in <i>Escherichia coli</i>

Lüttmann, Denise; Göpel, Yvonne; Görke, Boris

doi:10.1111/j.1365-2958.2012.08176.x

Cited by 60 publications

(72 citation statements)

References 48 publications

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“…Comparison of mutants lacking EIIA Ntr with mutants deficient for phosphorylation suggested that nonphosphorylated EIIA Ntr modulates the expression of pho. In addition, EIIA Ntr was found to bind directly to the sensor kinase PhoR and, through this interaction, to increase the amount of the phosphorylated response regulator PhoB (443). Importantly, the phosphate starvation response was controlled by nitrogen-PTS independent from its effects on K ϩ uptake.…”

Section: Figmentioning

confidence: 90%

Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

Heeswijk¹,

Westerhoff

Boogerd³

2013

Microbiol Mol Biol Rev

228

246

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SUMMARY We present a comprehensive overview of the hierarchical network of intracellular processes revolving around central nitrogen metabolism in Escherichia coli . The hierarchy intertwines transport, metabolism, signaling leading to posttranslational modification, and transcription. The protein components of the network include an ammonium transporter (AmtB), a glutamine transporter (GlnHPQ), two ammonium assimilation pathways (glutamine synthetase [GS]-glutamate synthase [glutamine 2-oxoglutarate amidotransferase {GOGAT}] and glutamate dehydrogenase [GDH]), the two bifunctional enzymes adenylyl transferase/adenylyl-removing enzyme (ATase) and uridylyl transferase/uridylyl-removing enzyme (UTase), the two trimeric signal transduction proteins (GlnB and GlnK), the two-component regulatory system composed of the histidine protein kinase nitrogen regulator II (NRII) and the response nitrogen regulator I (NRI), three global transcriptional regulators called nitrogen assimilation control (Nac) protein, leucine-responsive regulatory protein (Lrp), and cyclic AMP (cAMP) receptor protein (Crp), the glutaminases, and the nitrogen-phosphotransferase system. First, the structural and molecular knowledge on these proteins is reviewed. Thereafter, the activities of the components as they engage together in transport, metabolism, signal transduction, and transcription and their regulation are discussed. Next, old and new molecular data and physiological data are put into a common perspective on integral cellular functioning, especially with the aim of resolving counterintuitive or paradoxical processes featured in nitrogen assimilation. Finally, we articulate what still remains to be discovered and what general lessons can be learned from the vast amounts of data that are available now.

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Section: Figmentioning

confidence: 90%

Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

Heeswijk¹,

Westerhoff

Boogerd³

2013

Microbiol Mol Biol Rev

228

246

View full text Add to dashboard Cite

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“…Deletion of ptsN lowers the expression of the pho regulon because in order to be fully active, the sensor kinase PhoR needs to interact with EIIA Ntr . This activation seems to occur with unphosphorylated EIIA Ntr , because mutants unable to phosphorylate the EIIA component also exhibited increased expression of the pho regulon (128).…”

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

confidence: 99%

“…Another E. coli sensor kinase that was reported to be regulated by EIIA Ntr is PhoR (128). Together with the response regulator PhoB, PhoR controls the expression of the pho regulon, which includes more than 30 genes organized in nine transcription units.…”

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

341

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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“…9-11 Several regulatory roles of the nitrogen PTS were revealed in some bacteria. [12][13][14][15][16][17] The state of phosphorylation of proteins in this system is also crucial to the regulation phenomena.…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation-Dependent Mobility Shift of Proteins on SDS-PAGE is Due to Decreased Binding of SDS

Lee¹,

Park²,

Kim³

et al. 2013

Bulletin of the Korean Chemical Society

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While many eukaryotic and some prokaryotic proteins show a phosphorylation-dependent mobility shift (PDMS) on SDS-PAGE, the molecular mechanism for this phenomenon had not been elucidated. We have recently shown that the distribution of negatively charged amino acids around the phosphorylation site is important for the PDMS of some proteins. Here, we show that replacement of the phosphorylation site with a negatively charged amino acid results in a similar degree of the mobility shift of a protein as phosphorylation, indicating that the PDMS is due to the introduction of a negative charge by phosphorylation. Compared with a protein showing no shift, one showing a retarded mobility on SDS-PAGE had a decreased capacity for SDS binding. The elucidation of the consensus sequence (ΘX 1-3 ΘX 1-3 Θ, where Θ corresponds to an acidic function) for a PDMS suggests a general strategy for mutagenizing a phosphorylatable protein resulting in a PDMS.

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The phosphotransferase protein EIIA^Ntr modulates the phosphate starvation response through interaction with histidine kinase PhoR in Escherichia coli

Cited by 60 publications

References 48 publications

Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

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

Phosphorylation-Dependent Mobility Shift of Proteins on SDS-PAGE is Due to Decreased Binding of SDS

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The phosphotransferase protein EIIANtr modulates the phosphate starvation response through interaction with histidine kinase PhoR in Escherichia coli

Cited by 60 publications

References 48 publications

Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

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

Phosphorylation-Dependent Mobility Shift of Proteins on SDS-PAGE is Due to Decreased Binding of SDS

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The phosphotransferase protein EIIA^Ntr modulates the phosphate starvation response through interaction with histidine kinase PhoR in Escherichia coli