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

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Titel: SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features
Autoren: Lucas Gewehr, Benedikt Junglas, Ruven Jilly, Johannes Franz, Wenyu Eva Zhu, Tobias Weidner, Mischa Bonn, Carsten Sachse, Dirk Schneider
Weitere Verfasser: Johannes Gutenberg-Universität Mainz
Quelle: Nat Commun
Nature Communications, Vol 14, Iss 1, Pp 1-17 (2023)
Nature Communications
Nature Communications 14(1), 2156 (2023). doi:10.1038/s41467-023-37746-9
Gewehr, L, Junglas, B, Jilly, R, Franz, J, Zhu, W E, Weidner, T, Bonn, M, Sachse, C & Schneider, D 2023, 'SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features', Nature Communications, vol. 14, 2156. https://doi.org/10.1038/s41467-023-37746-9
Verlagsinformationen: Springer Science and Business Media LLC, 2023.
Publikationsjahr: 2023
Schlagwörter: Dynamins, 540 Chemistry and allied sciences, ddc:540, Science, Thylakoids, Article, GTP Phosphohydrolases, 570 Life sciences, Eukaryotic Cells/metabolism, Thylakoids/metabolism, Bacterial Proteins, Synechocystis/genetics, Dynamins/metabolism, Bacterial Proteins/genetics, Synechocystis, Eukaryota, GTP Phosphohydrolases/genetics, Eukaryota/metabolism, Eukaryotic Cells, 540 Chemie, ddc:570, 570 Biowissenschaften
Beschreibung: 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.
Publikationsart: Article
Other literature type
Dateibeschreibung: application/pdf
Sprache: English
ISSN: 2041-1723
DOI: 10.1038/s41467-023-37746-9
DOI: 10.25358/openscience-9637
Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/37059718
https://doaj.org/article/6620f236a7994b4e9ceb79427a9499db
https://openscience.ub.uni-mainz.de/handle/20.500.12030/9655
https://doi.org/10.25358/openscience-9637
http://hdl.handle.net/21.11116/0000-000D-05E4-C
http://hdl.handle.net/21.11116/0000-000D-05E6-A
https://juser.fz-juelich.de/record/1006880
Rights: CC BY
URL: http://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (http://creativecommons.org/licenses/by/4.0/) .
Dokumentencode: edsair.doi.dedup.....57a0669345e29cc2e2bb549583ecbd78
Datenbank: OpenAIRE
Beschreibung
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.
ISSN:20411723
DOI:10.1038/s41467-023-37746-9