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Cited by 6Cellular transport and secretionLipid Membrane Structure and BehaviorAdvanced Electron Microscopy Techniques and Applications

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

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Gewehr, Lucas, Junglas, Benedikt, Jilly, Ruven, Franz, Johannes, Zhu, Wenyu Eva, Weidner, Tobias, Bonn, Mischa, Sachse, Carsten, Schneider, Dirk·2023·Nature Communications
DOI 10.1038/s41467-023-37746-9PMC PMC10104851

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Abstract

Dynamin-like proteins are membrane remodeling GTPases with well-understood functions in eukaryotic cells. However, bacterial dynamin-like proteins are still poorly investigated. Syn DLP, 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 Syn DLP 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 Syn DLP. Furthermore, we show that Syn DLP interacts with and intercalates into membranes containing negatively charged thylakoid membrane lipids independent of nucleotides. The structural characteristics of Syn DLP oligomers suggest it to be the closest known bacterial ancestor of eukaryotic dynamin.

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Metadata

Authors
Gewehr, L., Junglas, B., Jilly, R., Franz, J., Zhu, W. E., Weidner, T., Bonn, M., Sachse, C., & Schneider, D.
Affiliations
  • Johannes Gutenberg University Mainz (DE)
  • Forschungszentrum Jülich (DE)
  • Max Planck Institute for Polymer Research (DE)
  • Aarhus University (DK)
Corresponding author
  • Sachse, Carsten
  • Schneider, Dirk
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2023-04-14
Volume
14
Issue
1
Pages
2156-2156
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-023-37746-9
PMC
PMC10104851
OpenAlex
W4365503926
Cited by
6
References
2
Citations by year
2025: 3 · 2024: 2 · 2023: 1
FWCI
0.87
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • Research Square (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Gutenberg Open Science (publishedVersion, cc-by)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Gutenberg Open Science (cc-by)
Funders
Max-Planck Graduate Center at the Max Planck institutes and the University of Mainz
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
Keywords
dynamin-like protein, Synechocystis sp. PCC 6803, cyanobacteria, GTPase, membrane remodeling, oligomerization, cryo-EM structure, intramolecular disulfide bridge, thylakoid membranes, membrane intercalation
MeSH terms
Bacterial Proteins, Eukaryotic Cells, Thylakoids, GTP Phosphohydrolases, Dynamins, Synechocystis, Eukaryota

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