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

Author

Listed:
  • Lucas Gewehr

    (Johannes Gutenberg University Mainz)

  • Benedikt Junglas

    (Ernst Ruska-Centre for Microscopy and Spectroscopy with Electrons (ER-C-3): Structural Biology
    Institute for Biological Information Processing (IBI-6): Cellular 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
    Institute for Biological Information Processing (IBI-6): Cellular Structural Biology
    Heinrich Heine University)

  • Dirk Schneider

    (Johannes Gutenberg University Mainz
    Johannes Gutenberg University Mainz)

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.

Suggested Citation

  • Lucas Gewehr & Benedikt Junglas & Ruven Jilly & Johannes Franz & Wenyu Eva Zhu & Tobias Weidner & Mischa Bonn & Carsten Sachse & Dirk Schneider, 2023. "SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-37746-9
    DOI: 10.1038/s41467-023-37746-9
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    References listed on IDEAS

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