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Bactofilins, a ubiquitous class of cytoskeletal proteins mediating polar localization of a cell wall synthase in Caulobacter crescentus

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Kühn,  Juliane
Max Planck Fellow Bacterial Cell Biology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Kahnt,  Jörg
Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Leser,  Katja
Max Planck Fellow Bacterial Cell Biology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Wick,  Stephanie
Max Planck Fellow Bacterial Cell Biology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Thanbichler,  Martin
Max Planck Fellow Bacterial Cell Biology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Kühn, J., Briegel, A., Mörschel, E., Kahnt, J., Leser, K., Wick, S., et al. (2010). Bactofilins, a ubiquitous class of cytoskeletal proteins mediating polar localization of a cell wall synthase in Caulobacter crescentus. The EMBO Journal, 29, 327-339. doi:10.1038/emboj.2009.358.


Cite as: https://hdl.handle.net/21.11116/0000-0007-C41F-A
Abstract
The cytoskeleton has a key function in the temporal and spatial organization of both prokaryotic and eukaryotic cells. Here, we report the identification of a new class of polymer-forming proteins, termed bactofilins, that are widely conserved among bacteria. In Caulobacter crescentus, two bactofilin paralogues cooperate to form a sheet-like structure lining the cytoplasmic membrane in proximity of the stalked cell pole. These assemblies mediate polar localization of a peptidoglycan synthase involved in stalk morphogenesis, thus complementing the function of the actin-like cytoskeleton and the cell division machinery in the regulation of cell wall biogenesis. In other bacteria, bactofilins can establish rod-shaped filaments or associate with the cell division apparatus, indicating considerable structural and functional flexibility. Bactofilins polymerize spontaneously in the absence of additional cofactors in vitro, forming stable ribbon- or rod-like filament bundles. Our results suggest that these structures have evolved as an alternative to intermediate filaments, s