The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions
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- Josef Deutscher
- Centre National de la Recherche Scientifique, FRE3630 Expression Génétique Microbienne, Institut de Biologie Physico-Chimique, Paris, France
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- Francine Moussan Désirée Aké
- INRA, Microbiologie de l'Alimentation au Service de la Santé Humaine, UMR1319, Jouy en Josas, France
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- Meriem Derkaoui
- INRA, Microbiologie de l'Alimentation au Service de la Santé Humaine, UMR1319, Jouy en Josas, France
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- Arthur Constant Zébré
- INRA, Microbiologie de l'Alimentation au Service de la Santé Humaine, UMR1319, Jouy en Josas, France
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- Thanh Nguyen Cao
- INRA, Microbiologie de l'Alimentation au Service de la Santé Humaine, UMR1319, Jouy en Josas, France
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- Houda Bouraoui
- INRA, Microbiologie de l'Alimentation au Service de la Santé Humaine, UMR1319, Jouy en Josas, France
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- Takfarinas Kentache
- INRA, Microbiologie de l'Alimentation au Service de la Santé Humaine, UMR1319, Jouy en Josas, France
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- Abdelhamid Mokhtari
- INRA, Microbiologie de l'Alimentation au Service de la Santé Humaine, UMR1319, Jouy en Josas, France
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- Eliane Milohanic
- INRA, Microbiologie de l'Alimentation au Service de la Santé Humaine, UMR1319, Jouy en Josas, France
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- Philippe Joyet
- INRA, Microbiologie de l'Alimentation au Service de la Santé Humaine, UMR1319, Jouy en Josas, France
抄録
<jats:title>SUMMARY</jats:title> <jats:p>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.</jats:p>
収録刊行物
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- Microbiology and Molecular Biology Reviews
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Microbiology and Molecular Biology Reviews 78 (2), 231-256, 2014-06
American Society for Microbiology