TY  - JOUR
AU  - Junglas, Benedikt
AU  - Gewehr, Lucas
AU  - Jilly, Ruven
AU  - Franz, Johannes
AU  - Zu, Whenju Eva
AU  - Weidner, Tobias
AU  - Bonn, Mischa
AU  - Sachse, Carsten
AU  - Schneider, Dirk
TI  - SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features
JO  - Nature Communications
VL  - 14
IS  - 1
SN  - 2041-1723
CY  - [London]
PB  - Nature Publishing Group UK
M1  - FZJ-2023-01912
SP  - 2156
PY  - 2023
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 37059718
UR  - <Go to ISI:>//WOS:000969250300022
DO  - DOI:10.1038/s41467-023-37746-9
UR  - https://juser.fz-juelich.de/record/1006880
ER  -