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Prokaryotic origin of the actin cytoskeleton

Nature volume 413, pages 39–44 (2001)Cite this article

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.

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Figure 1: MreB polymerization assays.
Figure 2: Electron micrographs of negatively stained MreB filaments.
Figure 3: Ribbon representation of the crystal structure of MreB complexed with AMPPNP and magnesium.
Figure 4: Sequence alignment of MreB1 from T. maritima to B. subtilis MreB (SWISSPROT: MREB_BACSU) and structure-based sequence alignment to yeast actin (SWISSPROT: ACT_YEAST; PDB, 1YAG) using DALI21.
Figure 5: Both crystal forms (HRES, NATI) contain one-dimensional protofilaments.
Figure 6: Close-up of the protofilament protein interface.

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Acknowledgements

We would like to thank S. Munro for critically reading the manuscript and the staff at ID14-4 of ESRF (Grenoble, France) for assistance with MAD data collection.

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  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Fusinita van den Ent, Linda A. Amos & Jan Löwe

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Correspondence to Fusinita van den Ent.

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van den Ent, F., Amos, L. & Löwe, J. Prokaryotic origin of the actin cytoskeleton. Nature 413, 39–44 (2001). https://doi.org/10.1038/35092500

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