| Literature DB >> 19959992 |
Juliane Kühn1, Ariane Briegel, Erhard Mörschel, Jörg Kahnt, Katja Leser, Stephanie Wick, Grant J Jensen, Martin Thanbichler.
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, serving as versatile molecular scaffolds in a variety of cellular pathways.Entities:
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Year: 2009 PMID: 19959992 PMCID: PMC2824468 DOI: 10.1038/emboj.2009.358
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598