SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features

Lucas Gewehr, Benedikt Junglas, Ruven Jilly, Johannes Franz, Wenyu Eva Zhu, Tobias Weidner, Mischa Bonn, Carsten Sachse () and Dirk Schneider ()
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Lucas Gewehr: Johannes Gutenberg University Mainz
Benedikt Junglas: Ernst Ruska-Centre for Microscopy and Spectroscopy with Electrons (ER-C-3): Structural Biology
Ruven Jilly: Johannes Gutenberg University Mainz
Johannes Franz: Max Planck Institute for Polymer Research
Wenyu Eva Zhu: Johannes Gutenberg University Mainz
Tobias Weidner: Department of Chemistry, Aarhus University
Mischa Bonn: Max Planck Institute for Polymer Research
Carsten Sachse: Ernst Ruska-Centre for Microscopy and Spectroscopy with Electrons (ER-C-3): Structural Biology
Dirk Schneider: Johannes Gutenberg University Mainz

Nature Communications, 2023, vol. 14, issue 1, 1-17

Abstract: Abstract Dynamin-like proteins are membrane remodeling GTPases with well-understood functions in eukaryotic cells. However, bacterial dynamin-like proteins are still poorly investigated. SynDLP, the dynamin-like protein of the cyanobacterium Synechocystis sp. PCC 6803, forms ordered oligomers in solution. The 3.7 Å resolution cryo-EM structure of SynDLP oligomers reveals the presence of oligomeric stalk interfaces typical for eukaryotic dynamin-like proteins. The bundle signaling element domain shows distinct features, such as an intramolecular disulfide bridge that affects the GTPase activity, or an expanded intermolecular interface with the GTPase domain. In addition to typical GD-GD contacts, such atypical GTPase domain interfaces might be a GTPase activity regulating tool in oligomerized SynDLP. Furthermore, we show that SynDLP interacts with and intercalates into membranes containing negatively charged thylakoid membrane lipids independent of nucleotides. The structural characteristics of SynDLP oligomers suggest it to be the closest known bacterial ancestor of eukaryotic dynamin.

Date: 2023
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DOI: 10.1038/s41467-023-37746-9

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