Prokaryotic origin of the actin cytoskeleton
Fusinita van den Ent (),
Linda A. Amos and
Jan Löwe
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Fusinita van den Ent: MRC Laboratory of Molecular Biology
Linda A. Amos: MRC Laboratory of Molecular Biology
Jan Löwe: MRC Laboratory of Molecular Biology
Nature, 2001, vol. 413, issue 6851, 39-44
Abstract:
Abstract It was thought until recently that bacteria lack the actin or tubulin filament networks that organize eukaryotic cytoplasm. However, we show here that the bacterial MreB protein assembles into filaments with a subunit repeat similar to that of F-actin—the physiological polymer of eukaryotic actin. By elucidating the MreB crystal structure we demonstrate that MreB and actin are very similar in three dimensions. Moreover, the crystals contain protofilaments, allowing visualization of actin-like strands at atomic resolution. The structure of the MreB protofilament is in remarkably good agreement with the model for F-actin, showing that the proteins assemble in identical orientations. The actin-like properties of MreB explain the finding that MreB forms large fibrous spirals under the cell membrane of rod-shaped cells, where they are involved in cell-shape determination. Thus, prokaryotes are now known to possess homologues both of tubulin, namely FtsZ, and of actin.
Date: 2001
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DOI: 10.1038/35092500
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