Structural insights into the signalling mechanisms of two-component systems

Jacob, Francoise; Mechaly, Ariel; Betton, Jean-Michel; Antoine, Rudy

Type de document :

Article dans une revue scientifique: Article original

DOI :

10.1038/s41579-018-0055-7

PMID :

30008469

Titre :

Structural insights into the signalling mechanisms of two-component systems

Auteur(s) :

Jacob, Francoise [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Mechaly, Ariel [Auteur]
Cristallographie (Plateforme) - Crystallography (Platform)
Betton, Jean-Michel [Auteur]
Microbiologie structurale - Structural Microbiology [Microb. Struc. (UMR_3528 / U-Pasteur_5)]
Antoine, Rudy [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]

Titre de la revue :

NATURE REVIEWS MICROBIOLOGY

Pagination :

585-593

Éditeur :

Nature Publishing Group

Date de publication :

2018-10

ISSN :

1740-1526

Discipline(s) HAL :

Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM]

Résumé en anglais : [en]

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. ...
Lire la suite >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.Lire moins >

Langue :

Anglais

Comité de lecture :

Oui

Audience :

Internationale

Vulgarisation :

Non

Projet ANR :

La Sécrétion à Deux Partenaires chez les bactéries : dynamique conformationnelle du transporteur FhaC.

Collections :

Centre d'Infection et d'Immunité de Lille (CIIL) - U1019 - UMR 9017

Source :

Harvested from HAL

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