Autoren:	Gewehr, Lucas Junglas, Benedikt Jilly, Ruven Franz, Johannes Zhu, Wenyu Eva Weidner, Tobias Bonn, Mischa Sachse, Carsten Schneider, Dirk
Titel:	SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features
Online-Publikationsdatum:	24-Okt-2023
Erscheinungsdatum:	2023
Sprache des Dokuments:	Englisch
Zusammenfassung/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-Sachgruppe:	540 Chemie 540 Chemistry and allied sciences 570 Biowissenschaften 570 Life sciences
Veröffentlichende Institution:	Johannes Gutenberg-Universität Mainz
Organisationseinheit:	FB 09 Chemie, Pharmazie u. Geowissensch.
Veröffentlichungsort:	Mainz
ROR:	https://ror.org/023b0x485
DOI:	http://doi.org/10.25358/openscience-9637
Version:	Published version
Publikationstyp:	Zeitschriftenaufsatz
Weitere Angaben zur Dokumentart:	Scientific article
Nutzungsrechte:	CC BY
Informationen zu den Nutzungsrechten:	https://creativecommons.org/licenses/by/4.0/
Zeitschrift:	Nature Communications 14
Seitenzahl oder Artikelnummer:	2156
Verlag:	Springer Nature
Verlagsort:	London
Erscheinungsdatum:	2023
ISSN:	2041-1723
DOI der Originalveröffentlichung:	10.1038/s41467-023-37746-9
Enthalten in den Sammlungen:	DFG-491381577-G