Journal Article

FZJ-2023-01912

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features

Junglas, B.FZJ* ; Gewehr, L. ; Jilly, R. ; Franz, J. ; Zu, W. E. ; Weidner, T. ; Bonn, M. ; Sachse, C. (Corresponding author)FZJ* ; Schneider, D. (Corresponding author)

2023
Nature Publishing Group UK [London]

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Please use a persistent id in citations: http://hdl.handle.net/2128/34332  doi:10.1038/s41467-023-37746-9

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.

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Contributing Institute(s):

1. Strukturbiologie (ER-C-3)

Research Program(s):

1. 5352 - Understanding the Functionality of Soft Matter and Biomolecular Systems (POF4-535) (POF4-535)
2. 5241 - Molecular Information Processing in Cellular Systems (POF4-524) (POF4-524)

Appears in the scientific report 2023

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