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Structure of a mitochondrial fission dynamin in the closed conformation

Olga Bohuszewicz1, Harry H Low2

  • 1Department of Life Sciences, Imperial College, London, UK.

Nature Structural & Molecular Biology
|August 1, 2018
PubMed

Insights

Dynamin 1-like proteins (DNM1-L) drive membrane fission. Researchers determined the crystal structure of algal CmDnm1, revealing a closed conformation suggesting an inactive state, distinct from other dynamins.

Area of Science:

  • Structural Biology
  • Cell Biology
  • Biochemistry

Background:

  • Dynamin 1-like proteins (DNM1-L) are essential GTPases mediating membrane fission in organelles like mitochondria and peroxisomes.
  • Their function relies on dynamic conformational changes influenced by nucleotide binding and lipid interactions.
  • Understanding these conformational states is crucial for elucidating the mechanism of membrane fission.

Purpose of the Study:

  • To determine the high-resolution crystal structure of a mitochondrial fission dynamin, CmDnm1, from the alga Cyanidioschyzon merolae.
  • To investigate the structural basis of CmDnm1's conformation and its implications for membrane fission.
  • To compare the structure of CmDnm1 with other eukaryotic dynamins and explore its functional relevance.

Main Methods:

  • X-ray crystallography was employed to obtain the crystal structure of CmDnm1.
  • Biochemical assays including crosslinking and photoinduced electron transfer were used for verification.
  • Transmission electron microscopy (TEM) was utilized to visualize protein assemblies.

Main Results:

  • The crystal structure revealed CmDnm1 in a hinge 1 closed conformation, with the GTPase domain tightly packed against the stalk.
  • CmDnm1 crystallized as a diamond-shaped tetramer, indicative of an inactive, off-membrane state.
  • In vitro experiments showed CmDnm1 forming concentration-dependent rings and protein-lipid tubes, similar to DNM1-L and classical dynamin in an open conformation.

Conclusions:

  • The closed hinge 1 conformation represents a key structural state potentially involved in regulating dynamin activity.
  • The findings suggest a mechanism for filament collapse and membrane release applicable to other dynamin family members.
  • CmDnm1's structural plasticity highlights the diverse mechanisms employed by dynamins in membrane fission.

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