An outer membrane porin-lipoprotein complex modulates elongasome movement to establish cell curvature in Rhodospirillum rubrum

Author:

Pöhl SebastianORCID,Giacomelli Giacomo,Meyer Fabian M.,Kleeberg Volker,Cohen Eli J.,Biboy Jacob,Rosum Julia,Glatter TimoORCID,Vollmer Waldemar,van Teeseling Muriel C. F.,Heider Johann,Bramkamp MarcORCID,Thanbichler MartinORCID

Abstract

AbstractCurved cell shapes are widespread among bacteria and important for cellular motility, virulence and fitness. However, the underlying morphogenetic mechanisms are still incompletely understood. Here, we identify an outer-membrane protein complex that promotes cell curvature in the photosynthetic species Rhodospirillum rubrum. We show that the R. rubrum porins Por39 and Por41 form a helical ribbon-like structure at the outer curve of the cell that recruits the peptidoglycan-binding lipoprotein PapS, with PapS inactivation, porin delocalization or disruption of the porin-PapS interface resulting in cell straightening. We further demonstrate that porin-PapS assemblies act as molecular cages that entrap the cell elongation machinery, thus biasing cell growth towards the outer curve. These findings reveal a mechanistically distinct morphogenetic module mediating bacterial cell shape. Moreover, they uncover an unprecedented role of outer-membrane protein patterning in the spatial control of intracellular processes, adding an important facet to the repertoire of regulatory mechanisms in bacterial cell biology.

Funder

Max-Planck-Gesellschaft

Deutsche Forschungsgemeinschaft

Philipps-Universität Marburg

RCUK | Biotechnology and Biological Sciences Research Council

Publisher

Springer Science and Business Media LLC

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