Requirement of the dephospho‐form of enzyme IIANtr for derepression of Escherichia coli K‐12 ilvBN expression

Lee, Chang-Ro; Koo, Bon Chul; Cho, Seung-Hyon; Kim, Yu-Jung; Yoon, Mi–Jeong; Peterkofsky, Alan; Seok, Yeong‐Jae

doi:10.1111/j.1365-2958.2005.04834.x

Cited by 52 publications

(73 citation statements)

References 42 publications

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“…Although the nitrogen-PTS has been proposed to play a general role in nitrogen assimilation and to provide a link between carbon and nitrogen assimilation (257,259,429,430), recent evidence does not corroborate this view, at least not for E. coli. In particular, the phenotypes associated with a lack of ptsN were all shown to be due to the presence of a nonfunctional version of the ilvG gene encoding acetohydroxy acid synthase II (AHASII) (431).…”

Section: Figmentioning

confidence: 80%

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

Heeswijk¹,

Westerhoff

Boogerd³

2013

Microbiol Mol Biol Rev

232

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: 80%

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

Heeswijk¹,

Westerhoff

Boogerd³

2013

Microbiol Mol Biol Rev

232

246

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“…The rsd gene was replaced with a tetracycline-resistant cassette. Bacterial cells were grown as described previously (34).…”

Section: Methodsmentioning

confidence: 99%

HPr antagonizes the anti-σ ⁷⁰ activity of Rsd in Escherichia coli

Park

Lee

Choe

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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The bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) is a multicomponent system that participates in a variety of physiological processes in addition to the phosphorylation-coupled transport of numerous sugars. In Escherichia coli and other enteric bacteria, enzyme IIA Glc (EIIA Glc ) is known as the central processing unit of carbon metabolism and plays multiple roles, including regulation of adenylyl cyclase, the fermentation/respiration switch protein FrsA, glycerol kinase, and several non-PTS transporters, whereas the only known regulatory role of the E. coli histidine-containing phosphocarrier protein HPr is in the activation of glycogen phosphorylase. Because HPr is known to be more abundant than EIIA Glc in enteric bacteria, we assumed that there might be more regulatory mechanisms connected with HPr. The ligand fishing experiment in this study identified Rsd, an anti-sigma factor known to complex with σ 70 in stationary-phase cells, as an HPr-binding protein in E. coli. Only the dephosphorylated form of HPr formed a tight complex with Rsd and thereby inhibited complex formation between Rsd and σ 70. Dephosphorylated HPr, but not phosphorylated HPr, antagonized the inhibitory effect of Rsd on σ 70-dependent transcriptions both in vivo and in vitro, and also influenced the competition between σ 70 and σ S for core RNA polymerase in the presence of Rsd. Based on these data, we propose that the anti-σ 70 activity of Rsd is regulated by the phosphorylation state-dependent interaction of HPr with Rsd.glucose signaling | sigma factor competition | transcriptional regulation B y monitoring their environment, bacteria ensure the most appropriate response for each environment. One of the sensory systems for monitoring changes in nutrient availability is the phosphoenolpyruvate (PEP):sugar phosphotransferase system (PTS). The PTS is a multicomponent system that catalyzes the concomitant phosphorylation and translocation of numerous sugar substrates across the cytoplasmic membrane. This system consists of two general components, enzyme I (EI) and the histidine-containing phosphocarrier protein HPr, which are common to all PTS sugars, along with many sugar-specific components collectively known as enzyme IIs (EIIs) (1, 2).Each EII complex generally consists of three domains: one integral membrane domain forming the sugar translocation channel (EIIC) and two cytosolic domains (EIIA and EIIB). EI transfers a phosphoryl group from PEP to HPr, and HPr then transfers the phosphoryl group to the different EIIs. Each EII complex forms a cascade of phosphorylated intermediates, and in the presence of a PTS sugar, the EIIA and EIIB domains sequentially transfer the phosphate group from HPr to the incoming sugar. Thus, the phosphorylation states of the PTS components change depending on the availability of a PTS sugar substrate (3, 4).In addition to sugar uptake, the PTS plays an important role as a sensory transduction system to monitor nutritional changes, and its components are involved in the regula...

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“…One sensory transduction system monitoring availability of a certain group of carbon sources is the phosphoenolpyruvate:sugar phosphotransferase system (PTS) (1). In addition to concomitant transport and phosphorylation of sugars, PTSs take part in a variety of physiological processes through direct interactions with their target proteins (2)(3)(4)(5).…”

mentioning

confidence: 99%

Analyses of Mlc–IIB ^Glc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration

Nam

Jung

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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In Escherichia coli, glucose-dependent transcriptional induction of genes encoding a variety of sugar-metabolizing enzymes and transport systems is mediated by the phosphorylation state-dependent interaction of membrane-bound enzyme IICB Glc (EIICB Glc ) with the global repressor Mlc. Here we report the crystal structure of a tetrameric Mlc in a complex with four molecules of enzyme IIB Glc (EIIB), the cytoplasmic domain of EIICB Glc . Each monomer of Mlc has one bound EIIB molecule, indicating the 1:1 stoichiometry. The detailed view of the interface, along with the high-resolution structure of EIIB containing a sulfate ion at the phosphorylation site, suggests that the phosphorylation-induced steric hindrance and disturbance of polar intermolecular interactions impede complex formation. Furthermore, we reveal that Mlc possesses a built-in flexibility for the structural adaptation to its target DNA and that interaction of Mlc with EIIB fused only to dimeric proteins resulted in the loss of its DNA binding ability, suggesting that flexibility of the Mlc structure is indispensable for its DNA binding.enzyme IICB Glc ͉ glucose signaling ͉ protein-protein interaction ͉ transcription regulation B acteria sense continuous changes in their environment and adapt metabolically to compete effectively with other organisms for limiting nutrients. One sensory transduction system monitoring availability of a certain group of carbon sources is the phosphoenolpyruvate:sugar phosphotransferase system (PTS) (1). In addition to concomitant transport and phosphorylation of sugars, PTSs take part in a variety of physiological processes through direct interactions with their target proteins (2-5).It is a normal occurrence that cells make more proteins necessary to transport and metabolize PTS sugars when they encounter an environment where PTS sugars are available. Glucose, a representative PTS sugar, mediates transcriptional activation of several genes for PTS-related sugar transporters and some enzymes involved in glycolysis (1, 6). Mlc, a tetrameric protein (7), is a signaling mediator for glucose induction of several PTS operons and related genes (8)(9)(10)(11)(12)(13)(14).A unique feature of induction of the Mlc regulon by glucose is that the effector molecule modulating Mlc activity is a membranebound protein, EIICB Glc (7,15,16), in which cytosolic EIIB protein is attached to membrane-embedded EIIC protein through a linker of Ͼ20 aa. In the absence of glucose, EIICB Glc mainly exists in the phosphorylated form (pEIICB Glc ). Because Mlc cannot interact with pEIICB Glc , Mlc dissociates from pEIICB Glc to bind to target promoters and repress their transcription. When glucose is available, transported glucose takes the phospho-groups away from pEIICB Glc and the dephosphorylated EIICB Glc recruits Mlc to sequester it from its target promoters. This leads to increased synthesis of EIICB Glc and other PTS proteins necessary to take up and metabolize glucose more efficiently.The physiological importance of the glucose-specific enz...

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Requirement of the dephospho‐form of enzyme IIA^Ntr for derepression of Escherichia coli K‐12 ilvBN expression

Cited by 52 publications

References 42 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

HPr antagonizes the anti-σ ⁷⁰ activity of Rsd in Escherichia coli

Analyses of Mlc–IIB ^Glc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration

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Requirement of the dephospho‐form of enzyme IIANtr for derepression of Escherichia coli K‐12 ilvBN expression

Cited by 52 publications

References 42 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

HPr antagonizes the anti-σ 70 activity of Rsd in Escherichia coli

Analyses of Mlc–IIB Glc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration

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Requirement of the dephospho‐form of enzyme IIA^Ntr for derepression of Escherichia coli K‐12 ilvBN expression

HPr antagonizes the anti-σ ⁷⁰ activity of Rsd in Escherichia coli

Analyses of Mlc–IIB ^Glc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration