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Related Experiment Videos

The dynamin A ring complex: molecular organization and nucleotide-dependent conformational changes.

Boris Klockow1, Willem Tichelaar, Dean R Madden

  • 1Department of Biophysics, Max-Planck-Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany.

The EMBO Journal
|February 2, 2002
PubMed
Summary

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Dictyostelium discoideum dynamin A, a fast GTPase, self-assembles into rings and helices. Modifications stabilize a ring complex, revealing its molecular organization and mechanochemical action in membrane fission.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Structural Biology

Background:

  • Dynamins are GTPases crucial for membrane dynamics.
  • Human dynamin-1 self-assembles into rings and helices.
  • Understanding dynamin assembly is key to membrane fission mechanisms.

Purpose of the Study:

  • To investigate the self-assembly properties of Dictyostelium discoideum dynamin A.
  • To determine the molecular organization of dynamin A complexes.
  • To elucidate the role of specific domains in dynamin assembly and function.

Main Methods:

  • Biochemical assays to study GTPase activity and lipid binding.
  • Chemical modification of cysteine residues.
  • Single particle analysis for 3D structural determination.

Related Experiment Videos

  • Nucleotide-binding studies.

    • Main Results:

    • Dictyostelium dynamin A is a fast GTPase that binds negatively charged lipids.
    • It self-assembles into nucleotide-dependent rings and helices.
    • Modified dynamin A stabilizes a regular ring complex with 11-fold symmetry.
    • 3D reconstruction reveals a two-layered nucleotide-free complex.

    Conclusions:

    • The middle domain and GTPase effector domain (GED) are critical for dynamin assembly.
    • Nucleotide-dependent conformational changes support a mechanochemical model of membrane fission.
    • Dynamin A shares functional and structural similarities with human dynamin-1.