The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism.
Fiche publication
Date publication
mars 2020
Journal
Nature communications
Auteurs
Membres identifiés du Cancéropôle Est :
Dr RASSAM Patrice
Tous les auteurs :
Szczepaniak J, Holmes P, Rajasekar K, Kaminska R, Samsudin F, Inns PG, Rassam P, Khalid S, Murray SM, Redfield C, Kleanthous C
Lien Pubmed
Résumé
Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol system. Here, we show that Pal accumulation at Escherichia coli division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system.
Mots clés
Bacterial Outer Membrane, metabolism, Bacterial Outer Membrane Proteins, metabolism, Cell Division, Escherichia coli, cytology, Escherichia coli Proteins, metabolism, Lipoproteins, metabolism, Membrane Proteins, Peptidoglycan, metabolism, Periplasmic Proteins, metabolism
Référence
Nat Commun. 2020 03 11;11(1):1305