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Structure and function of a spectrin-like regulator of bacterial cytokinesis

Author

Listed:
  • Robert M. Cleverley

    (Institute for Cell and Molecular Biosciences, Newcastle University)

  • Jeffrey R. Barrett

    (Centre for Medical and Molecular Bioscience, University of Wollongong)

  • Arnaud Baslé

    (Institute for Cell and Molecular Biosciences, Newcastle University)

  • Nhat Khai Bui

    (Institute for Cell and Molecular Biosciences, Newcastle University
    Present address: Helmholtz Centre for Infection Research, Helmholtz Institute for Pharmaceutical Research, Saarland University, 66123 Saarbrücken, Germany)

  • Lorraine Hewitt

    (Institute for Cell and Molecular Biosciences, Newcastle University)

  • Alexandra Solovyova

    (NUPPA, Devonshire Building, Newcastle University)

  • Zhi-Qiang Xu

    (Centre for Medical and Molecular Bioscience, University of Wollongong)

  • Richard A. Daniel

    (Institute for Cell and Molecular Biosciences, Newcastle University)

  • Nicholas E. Dixon

    (Centre for Medical and Molecular Bioscience, University of Wollongong)

  • Elizabeth J. Harry

    (The ithree Institute, University of Technology)

  • Aaron J. Oakley

    (Centre for Medical and Molecular Bioscience, University of Wollongong)

  • Waldemar Vollmer

    (Institute for Cell and Molecular Biosciences, Newcastle University)

  • Richard J. Lewis

    (Institute for Cell and Molecular Biosciences, Newcastle University)

Abstract

Bacterial cell division is facilitated by a molecular machine—the divisome—that assembles at mid-cell in dividing cells. The formation of the cytokinetic Z-ring by the tubulin homologue FtsZ is regulated by several factors, including the divisome component EzrA. Here we describe the structure of the 60-kDa cytoplasmic domain of EzrA, which comprises five linear repeats of an unusual triple helical bundle. The EzrA structure is bent into a semicircle, providing the protein with the potential to interact at both N- and C-termini with adjacent membrane-bound divisome components. We also identify at least two binding sites for FtsZ on EzrA and map regions of EzrA that are responsible for regulating FtsZ assembly. The individual repeats, and their linear organization, are homologous to the spectrin proteins that connect actin filaments to the membrane in eukaryotes, and we thus propose that EzrA is the founding member of the bacterial spectrin family.

Suggested Citation

  • Robert M. Cleverley & Jeffrey R. Barrett & Arnaud Baslé & Nhat Khai Bui & Lorraine Hewitt & Alexandra Solovyova & Zhi-Qiang Xu & Richard A. Daniel & Nicholas E. Dixon & Elizabeth J. Harry & Aaron J. O, 2014. "Structure and function of a spectrin-like regulator of bacterial cytokinesis," Nature Communications, Nature, vol. 5(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6421
    DOI: 10.1038/ncomms6421
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