Structural insights into the signalling mechanisms of two-component systems
| Autor: | Françoise Jacob-Dubuisson, Ariel E. Mechaly, Jean-Michel Betton, Rudy Antoine |
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| Přispěvatelé: | Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Cristallographie (Plateforme) - Crystallography (Platform), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Microbiologie structurale - Structural Microbiology (Microb. Struc. (UMR_3528 / U-Pasteur_5)), Institut Pasteur [Paris]-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), The work in F.J.-D.’s group was supported by the Agence Nationale de la Recherche (grant ANR-10-BLAN-1306). The authors apologize to all colleagues whose excellent work on two-component systems could not be cited because of space limitations., The authors thank E. Pradel for carefully reading the manuscript. They also thank A. Buschiazzo, F. Trajtenberg and J. Imelio (Institut Pasteur of Montevideo) for kindly sharing the coordinates file of the DesK–DesR complex model shown in Fig. 2a., Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris] (IP)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Centre d’Infection et d’Immunité de Lille (CIIL) - U1019 - UMR 8204 (CIIL), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Cristallographie (Plate-forme) |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Cytoplasm Histidine Kinase MESH: Cytoplasm/metabolism 030106 microbiology Regulator MESH: Phosphorylation/physiology Biology Microbiology MESH: Histidine Kinase*/physiology 03 medical and health sciences MESH: Bacterial Proteins*/physiology Bacterial Proteins MESH: Bacteria/chemistry MESH: Bacterial Proteins*/chemistry Phosphorylation Histidine MESH: Histidine Kinase*/chemistry MESH: Bacterial Proteins*/metabolism Bacteria General Immunology and Microbiology [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Autophosphorylation Histidine kinase MESH: Histidine Kinase*/metabolism MESH: Cytoplasm/chemistry MESH: Bacteria/enzymology Molecular machine Transmembrane protein MESH: Signal Transduction/physiology [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] Response regulator 030104 developmental biology Infectious Diseases Biophysics Signal transduction MESH: Cytoplasm/physiology MESH: Models Molecular Signal Transduction MESH: Bacteria/metabolism |
| Zdroj: | Nature Reviews Microbiology Nature Reviews Microbiology, Nature Publishing Group, 2018, 16 (10), pp.585-593. ⟨10.1038/s41579-018-0055-7⟩ Nature Reviews Microbiology, 2018, 16 (10), pp.585-593. ⟨10.1038/s41579-018-0055-7⟩ |
| ISSN: | 1740-1526 1740-1534 |
| DOI: | 10.1038/s41579-018-0055-7⟩ |
| Popis: | International audience; Two-component systems reprogramme diverse aspects of microbial physiology in response to environmental cues. Canonical systems are composed of a transmembrane sensor histidine kinase and its cognate response regulator. They catalyse three reactions: autophosphorylation of the histidine kinase, transfer of the phosphoryl group to the regulator and dephosphorylation of the phosphoregulator. Elucidating signal transduction between sensor and output domains is highly challenging given the size, flexibility and dynamics of histidine kinases. However, recent structural work has provided snapshots of the catalytic mechanisms of the three enzymatic reactions and described the conformation and dynamics of the enzymatic moiety in the kinase-competent and phosphatase-competent states. Insight into signalling mechanisms across the membrane is also starting to emerge from new crystal structures encompassing both sensor and transducer domains of sensor histidine kinases. In this Progress article, we highlight such important advances towards understanding at the molecular level the signal transduction mechanisms mediated by these fascinating molecular machines. |
| Databáze: | OpenAIRE |
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