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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

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Volume 393, Issue 11


Structure and function of bacterial dynamin-like proteins

Marc Bramkamp
  • Corresponding author
  • Ludwig-Maximilians-University Munich, Biocenter, Department Biology I, Großhaderner Str. 2-4, D-82152 Planegg-Martinsried, Germany
  • University of Cologne, Department of Chemistry, Institute of Biochemistry, Zülpicher Str. 47, D-50674 Cologne, Germany
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Published Online: 2012-10-11 | DOI: https://doi.org/10.1515/hsz-2012-0185


Membrane dynamics are essential for numerous cellular processes in eukaryotic and prokaryotic cells. In eukaryotic cells, membrane fusion and fission are often catalyzed by large GTPases of the dynamin protein family. These proteins couple GTP hydrolysis to membrane deformation, which eventually leads to fusion or fission of the lipid bilayer. Mutations in eukaryotic dynamin-like proteins (DLPs) are associated with various diseases underscoring the importance to fully understand the biochemistry of these proteins. In recent years, a wealth of structural and biochemical data have been published that allow a detailed analysis of how dynamins or DLPs modulate biological membranes. However, less is known about the function of bacterial DLPs, although structural data exist. This review summarizes current knowledge about bacterial dynamins and discusses structural and functional properties in comparison to their eukaryotic counterparts.

Keywords: BDLP; cytokinesis; DynA; dynamin; fission; fusion; GTPase, membrane

About the article

Corresponding author: Marc Bramkamp, Ludwig-Maximilians-University Munich, Biocenter, Department Biology I, Großhaderner Str. 2-4, D-82152 Planegg-Martinsried, Germany; and University of Cologne, Department of Chemistry, Institute of Biochemistry, Zülpicher Str. 47, D-50674 Cologne, Germany

Received: 2012-04-23

Accepted: 2012-06-29

Published Online: 2012-10-11

Published in Print: 2012-11-01

Citation Information: , Volume 393, Issue 11, Pages 1203–1214, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2012-0185.

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©2012 by Walter de Gruyter Berlin Boston. Copyright Clearance Center

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