Glucose-Specific Enzyme IIA Has Unique Binding Partners in The Vibrio cholerae Biofilm

Pickering, Bradley; Smith, Daniel R.; Watnick, Paula I.

doi:10.1128/mbio.00228-12

Cited by 36 publications

(62 citation statements)

References 47 publications

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“…However, when adenylate cyclase activity assays were carried out in the presence of E. coli crude extracts, only PϳEIIA Glc was able to stimulate the enzyme activity (171). An interaction of unphosphorylated EIIA Glc with adenylate cyclase could also be demonstrated by in vivo experiments with the His-91-Ala EIIA Glc mutant from V. cholerae by using the tandem affinity purification method (102).…”

Section: Interaction With Phosphorylated Pts Proteinsmentioning

confidence: 95%

“…However, several other proteins were also found to interact with EIIA Glc . Interaction partners in planktonic cells include the glycolytic enzyme 6-phosphofructokinase, the purine repressor PurR, and a protein containing the GGDEF motif characteristic of diguanylate cyclases (VC0900) (102 (104). This protein is present in most facultative anaerobic gammaproteobacteria and is also found in a few alpha-and betaproteobacteria, such as Thauera selenatis and Hirschia maritima.…”

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

confidence: 99%

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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

329

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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Section: Interaction With Phosphorylated Pts Proteinsmentioning

confidence: 95%

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

329

374

View full text Add to dashboard Cite

show abstract

“…Other GGDEF or EAL domains of bacterial proteins have also evolved novel roles (81,82). A CsrD homolog in Vibrio cholerae, MshH, was found to interact with the glucose-specific enzyme IIA (EIIA Glc ) of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS), which is a central regulator of carbon metabolism (83). Whether carbon flux regulates CsrB/C RNA turnover through this interaction and which CsrD domain(s) is responsible for binding to EIIA Glc remain to be determined.…”

Section: Regulation Of the Csr/rsm Systemmentioning

confidence: 99%

Regulation of Bacterial Virulence by Csr (Rsm) Systems

Vakulskas

Potts

Babitzke

et al. 2015

Microbiol Mol Biol Rev

287

400

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SUMMARY Most bacterial pathogens have the remarkable ability to flourish in the external environment and in specialized host niches. This ability requires their metabolism, physiology, and virulence factors to be responsive to changes in their surroundings. It is no surprise that the underlying genetic circuitry that supports this adaptability is multilayered and exceedingly complex. Studies over the past 2 decades have established that the CsrA/RsmA proteins, global regulators of posttranscriptional gene expression, play important roles in the expression of virulence factors of numerous proteobacterial pathogens. To accomplish these tasks, CsrA binds to the 5′ untranslated and/or early coding regions of mRNAs and alters translation, mRNA turnover, and/or transcript elongation. CsrA activity is regulated by noncoding small RNAs (sRNAs) that contain multiple CsrA binding sites, which permit them to sequester multiple CsrA homodimers away from mRNA targets. Environmental cues sensed by two-component signal transduction systems and other regulatory factors govern the expression of the CsrA-binding sRNAs and, ultimately, the effects of CsrA on secretion systems, surface molecules and biofilm formation, quorum sensing, motility, pigmentation, siderophore production, and phagocytic avoidance. This review presents the workings of the Csr system, the paradigm shift that it generated for understanding posttranscriptional regulation, and its roles in virulence networks of animal and plant pathogens.

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“…The role of EIIA Glc in a particular growth condition is governed by its interactions with other proteins (22). We hypothesize that activation of biofilm formation by EIIA Glc in LB broth reflects its interaction with an as yet unexplored partner.…”

Section: ⌬Ei ⌬Mlc Mutants (A) a ⌬Eiibcmentioning

confidence: 99%

“…We recently determined that sugars transported by the PTS activate transcription of the vps genes and biofilm formation (17)(18)(19)(20). Furthermore, even in the absence of PTS substrates, the network of Vibrio cholerae PTS components forms a complex web that regulates vps gene transcription and biofilm formation through multiple independent pathways (2,(20)(21)(22)(23).…”

mentioning

confidence: 99%

The Transcription Factor Mlc Promotes Vibrio cholerae Biofilm Formation through Repression of Phosphotransferase System Components

et al. 2014

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The phosphoenol phosphotransferase system (PTS) is a multicomponent signal transduction cascade that regulates diverse aspects of bacterial cellular physiology in response to the availability of high-energy sugars in the environment. Many PTS components are repressed at the transcriptional level when the substrates they transport are not available. In Escherichia coli, the transcription factor Mlc (for makes large colonies) represses transcription of the genes encoding enzyme I (EI), histidine protein (HPr), and the glucose-specific enzyme IIBC (EIIBC Glc ) in defined media that lack PTS substrates. When glucose is present, the unphosphorylated form of EIIBC Glc sequesters Mlc to the cell membrane, preventing its interaction with DNA. Very little is known about Vibrio cholerae Mlc. We found that V. cholerae Mlc activates biofilm formation in LB broth but not in defined medium supplemented with either pyruvate or glucose. Therefore, we questioned whether V. cholerae Mlc functions differently than E. coli Mlc. Here we have shown that, like E. coli Mlc, V. cholerae Mlc represses transcription of PTS components in both defined medium and LB broth and that E. coli Mlc is able to rescue the biofilm defect of a V. cholerae ⌬mlc mutant. Furthermore, we provide evidence that Mlc indirectly activates transcription of the vps genes by repressing expression of EI. Because activation of the vps genes by Mlc occurs under only a subset of the conditions in which repression of PTS components is observed, we conclude that additional inputs present in LB broth are required for activation of vps gene transcription by Mlc.

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Glucose-Specific Enzyme IIA Has Unique Binding Partners in The Vibrio cholerae Biofilm

Cited by 36 publications

References 47 publications

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

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

Regulation of Bacterial Virulence by Csr (Rsm) Systems

The Transcription Factor Mlc Promotes Vibrio cholerae Biofilm Formation through Repression of Phosphotransferase System Components

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