Please use this identifier to cite or link to this item:
http://doi.org/10.25358/openscience-9637Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Gewehr, Lucas | - |
| dc.contributor.author | Junglas, Benedikt | - |
| dc.contributor.author | Jilly, Ruven | - |
| dc.contributor.author | Franz, Johannes | - |
| dc.contributor.author | Zhu, Wenyu Eva | - |
| dc.contributor.author | Weidner, Tobias | - |
| dc.contributor.author | Bonn, Mischa | - |
| dc.contributor.author | Sachse, Carsten | - |
| dc.contributor.author | Schneider, Dirk | - |
| dc.date.accessioned | 2023-10-24T08:17:13Z | - |
| dc.date.available | 2023-10-24T08:17:13Z | - |
| dc.date.issued | 2023 | - |
| dc.identifier.uri | https://openscience.ub.uni-mainz.de/handle/20.500.12030/9655 | - |
| dc.description.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. | en_GB |
| dc.description.sponsorship | Deutsche Forschungsgemeinschaft (DFG)|491381577|Open-Access-Publikationskosten 2022–2024 Universität Mainz - Universitätsmedizin | - |
| dc.language.iso | eng | de |
| dc.rights | CC BY | * |
| dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | * |
| dc.subject.ddc | 540 Chemie | de_DE |
| dc.subject.ddc | 540 Chemistry and allied sciences | en_GB |
| dc.subject.ddc | 570 Biowissenschaften | de_DE |
| dc.subject.ddc | 570 Life sciences | en_GB |
| dc.title | SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features | en_GB |
| dc.type | Zeitschriftenaufsatz | de |
| dc.identifier.doi | http://doi.org/10.25358/openscience-9637 | - |
| jgu.type.contenttype | Scientific article | de |
| jgu.type.dinitype | article | en_GB |
| jgu.type.version | Published version | de |
| jgu.type.resource | Text | de |
| jgu.organisation.department | FB 09 Chemie, Pharmazie u. Geowissensch. | de |
| jgu.organisation.number | 7950 | - |
| jgu.organisation.name | Johannes Gutenberg-Universität Mainz | - |
| jgu.rights.accessrights | openAccess | - |
| jgu.journal.title | Nature Communications | de |
| jgu.journal.volume | 14 | de |
| jgu.pages.alternative | 2156 | de |
| jgu.publisher.year | 2023 | - |
| jgu.publisher.name | Springer Nature | de |
| jgu.publisher.place | London | de |
| jgu.publisher.issn | 2041-1723 | de |
| jgu.organisation.place | Mainz | - |
| jgu.subject.ddccode | 540 | de |
| jgu.subject.ddccode | 570 | de |
| jgu.publisher.doi | 10.1038/s41467-023-37746-9 | de |
| jgu.organisation.ror | https://ror.org/023b0x485 | - |
| jgu.subject.dfg | Naturwissenschaften | de |
| Appears in collections: | DFG-491381577-G | |
Files in This Item:
| File | Description | Size | Format | ||
|---|---|---|---|---|---|
 | syndlp_is_a_dynaminlike_prote-20231024093747906.pdf | 4.62 MB | Adobe PDF | View/Open |