Mycobacterial dynamin-like protein IniA mediates membrane fission

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 () and Zihe Rao
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Manfu Wang: ShanghaiTech University
Xiangyang Guo: Nankai University, and Tianjin Key Laboratory of Protein Sciences
Xiuna Yang: ShanghaiTech University
Bing Zhang: ShanghaiTech University
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
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
Jun Li: ShanghaiTech University
Zihe Rao: ShanghaiTech University

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-11860-z

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