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Mycobacterial dynamin-like protein IniA mediates membrane fission

Manfu Wang1,2,3, Xiangyang Guo4, Xiuna Yang1,2

  • 1Shanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.

Nature Communications
|August 31, 2019
PubMed

Insights

Mycobacterium tuberculosis protein IniA, a bacterial dynamin-like protein (BDLP), undergoes GTP-dependent membrane fission. This activity may explain how IniA contributes to tuberculosis drug resistance by maintaining plasma membrane integrity.

Area of Science:

  • Structural biology
  • Molecular microbiology
  • Biochemistry

Background:

  • Mycobacterium tuberculosis infection is a global health threat.
  • Drug treatments upregulate mycobacterial proteins like IniA, whose function is unclear.
  • Understanding IniA is crucial for addressing tuberculosis drug resistance.

Purpose of the Study:

  • To elucidate the structure and function of Mycobacterium smegmatis IniA.
  • To investigate IniA's role in membrane interaction and remodeling.
  • To explore IniA's potential contribution to tuberculosis drug resistance.

Main Methods:

  • X-ray crystallography to determine IniA structures in nucleotide-free and GTP-bound states.
  • Biochemical assays to assess GTP hydrolysis and membrane binding.
  • Lipid-binding studies to identify IniA's membrane interaction interface.

Main Results:

  • IniA folds as a bacterial dynamin-like protein (BDLP) with distinct GTPase, Neck, and Trunk domains.
  • A lipid-interacting (LI) loop in the Trunk domain binds negatively charged lipids.
  • IniA mediates GTP-hydrolysis-dependent membrane fission, deforming membranes.

Conclusions:

  • IniA exhibits nucleotide-independent membrane association via lipid tethering.
  • IniA possesses membrane remodeling and fission capabilities, characteristic of BDLP.
  • IniA's fission activity may be key to maintaining plasma membrane integrity and conferring tuberculosis drug resistance.

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