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

Boris Klockow·Willem Tichelaar·Dean R Madden·Hartmut H Niemann·Toshihiko Akiba·Keiko Hirose·Dietmar J Manstein
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Abstract

Here we show that Dictyostelium discoideum dynamin A is a fast GTPase, binds to negatively charged lipids, and self-assembles into rings and helices in a nucleotide-dependent manner, similar to human dynamin-1. Chemical modification of two cysteine residues, positioned in the middle domain and GTPase effector domain (GED), leads to altered assembly properties and the stabilization of a highly regular ring complex. Single particle analysis of this dynamin A* ring complex led to a three-dimensional map, which shows that the nucleotide-free complex consists of two layers with 11-fold symmetry. Our results reveal the molecular organization of the complex and indicate the importance of the middle domain and GED for the assembly of dynamin family proteins. Nucleotide-dependent changes observed with the unmodified and modified protein support a mechanochemical action of dynamin, in which tightening and stretching of a helix contribute to membrane fission.

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AnimalsDictyosteliumDimerizationDynaminsGTP PhosphohydrolasesHumansProtein ConformationProtozoan ProteinsJournal ArticleResearch Support, Non-U.S. Gov't

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Boris Klockow, Willem Tichelaar, Dean R Madden, Hartmut H Niemann, Toshihiko Akiba, Keiko Hirose, Dietmar J Manstein. 2002-02-01. The dynamin A ring complex: molecular organization and nucleotide-dependent conformational changes.. https://doi.org/10.1093/emboj%2F21.3.240

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