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

Lookup NU author(s): Dr Susanne Pohl, Dr Jacob BiboyORCiD, Professor Waldemar Vollmer

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

© The Author(s) 2024.Curved 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.


Publication metadata

Author(s): Pohl S, Giacomelli G, Meyer FM, Kleeberg V, Cohen EJ, Biboy J, Rosum J, Glatter T, Vollmer W, van Teeseling MCF, Heider J, Bramkamp M, Thanbichler M

Publication type: Article

Publication status: Published

Journal: Nature Communications

Year: 2024

Volume: 15

Issue: 1

Online publication date: 02/09/2024

Acceptance date: 14/08/2024

Date deposited: 16/09/2024

ISSN (electronic): 2041-1723

Publisher: Nature Research

URL: https://doi.org/10.1038/s41467-024-51790-z

DOI: 10.1038/s41467-024-51790-z

Data Access Statement: The mass spectrometry proteomics data generated in this study have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD049473. All other data generated in this study are included in the manuscript or the supplementary material. Source data are provided with this paper.

PubMed id: 39223154


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