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Authors: Gewehr, Lucas
Junglas, Benedikt
Jilly, Ruven
Franz, Johannes
Zhu, Wenyu Eva
Weidner, Tobias
Bonn, Mischa
Sachse, Carsten
Schneider, Dirk
Title: SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features
Online publication date: 24-Oct-2023
Year of first publication: 2023
Language: english
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.
DDC: 540 Chemie
540 Chemistry and allied sciences
570 Biowissenschaften
570 Life sciences
Institution: Johannes Gutenberg-Universität Mainz
Department: FB 09 Chemie, Pharmazie u. Geowissensch.
Place: Mainz
Version: Published version
Publication type: Zeitschriftenaufsatz
Document type specification: Scientific article
License: CC BY
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Journal: Nature Communications
Pages or article number: 2156
Publisher: Springer Nature
Publisher place: London
Issue date: 2023
ISSN: 2041-1723
Publisher DOI: 10.1038/s41467-023-37746-9
Appears in collections:DFG-491381577-G

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