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- W4256407789 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. PMID: 11544518" @default.
- W4256407789 created "2022-05-12" @default.
- W4256407789 creator A5080323204 @default.
- W4256407789 date "2002-01-05" @default.
- W4256407789 modified "2023-09-30" @default.
- W4256407789 title "Faculty Opinions recommendation of Prokaryotic origin of the actin cytoskeleton." @default.
- W4256407789 doi "https://doi.org/10.3410/f.1000163.19558" @default.
- W4256407789 hasPublicationYear "2002" @default.
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