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Mycobacterial dynamin-like protein IniA mediates membrane fission

Author

Listed:
  • Manfu Wang

    (ShanghaiTech University
    CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Xiangyang Guo

    (Nankai University, and Tianjin Key Laboratory of Protein Sciences)

  • Xiuna Yang

    (ShanghaiTech University
    CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences)

  • Bing Zhang

    (ShanghaiTech University
    CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences)

  • Jie Ren

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Science)

  • Aijun Liu

    (Tsinghua University)

  • Yajun Ran

    (ShanghaiTech University
    CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences)

  • Bing Yan

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Science)

  • Fang Chen

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Science)

  • Luke W. Guddat

    (The University of Queensland)

  • Junjie Hu

    (Nankai University, and Tianjin Key Laboratory of Protein Sciences
    National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Science)

  • Jun Li

    (ShanghaiTech University
    CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences)

  • Zihe Rao

    (ShanghaiTech University
    Nankai University, and Tianjin Key Laboratory of Protein Sciences
    National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Science
    Tsinghua University)

Abstract

Mycobacterium tuberculosis infection remains a major threat to human health worldwide. Drug treatments against tuberculosis (TB) induce expression of several mycobacterial proteins, including IniA, but its structure and function remain poorly understood. Here, we report the structures of Mycobacterium smegmatis IniA in both the nucleotide-free and GTP-bound states. The structures reveal that IniA folds as a bacterial dynamin-like protein (BDLP) with a canonical GTPase domain followed by two helix-bundles (HBs), named Neck and Trunk. The distal end of its Trunk domain exists as a lipid-interacting (LI) loop, which binds to negatively charged lipids for membrane attachment. IniA does not form detectable nucleotide-dependent dimers in solution. However, lipid tethering indicates nucleotide-independent association of IniA on the membrane. IniA also deforms membranes and exhibits GTP-hydrolyzing dependent membrane fission. These results confirm the membrane remodeling activity of BDLP and suggest that IniA mediates TB drug-resistance through fission activity to maintain plasma membrane integrity.

Suggested Citation

  • Manfu Wang & Xiangyang Guo & Xiuna Yang & Bing Zhang & Jie Ren & Aijun Liu & Yajun Ran & Bing Yan & Fang Chen & Luke W. Guddat & Junjie Hu & Jun Li & Zihe Rao, 2019. "Mycobacterial dynamin-like protein IniA mediates membrane fission," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11860-z
    DOI: 10.1038/s41467-019-11860-z
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    Cited by:

    1. Lucas Gewehr & Benedikt Junglas & Ruven Jilly & Johannes Franz & Wenyu Eva Zhu & Tobias Weidner & Mischa Bonn & Carsten Sachse & Dirk Schneider, 2023. "SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

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