Evidence map›Paper›PMID 37059718›Full record

ArticleNature communications2023

SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features.

Lucas Gewehr, Benedikt Junglas, Ruven Jilly, Johannes Franz, Wenyu Eva Zhu, Tobias Weidner, Mischa Bonn, Carsten Sachse, Dirk Schneider

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.8field-weighted citation impact, top 28% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 5 institutions in 2 countries.

Lucas Gewehr *Department of Chemistry, Biochemistry, Johannes Gutenberg University Mainz, Mainz, Germany.
Benedikt Junglas *Ernst Ruska-Centre for Microscopy and Spectroscopy with Electrons (ER-C-3): Structural Biology, Jülich, Germany.ORCID 0000-0001-9348-3379
Ruven JillyDepartment of Chemistry, Biochemistry, Johannes Gutenberg University Mainz, Mainz, Germany.
Johannes FranzMax Planck Institute for Polymer Research, Ackermannweg 10, 55128, Mainz, Germany.
Wenyu Eva ZhuDepartment of Chemistry, Biochemistry, Johannes Gutenberg University Mainz, Mainz, Germany.
Tobias WeidnerDepartment of Chemistry, Aarhus University, Langelandsgade 140, 8000, Aarhus C, Denmark.ORCID 0000-0002-7083-7004
Mischa BonnMax Planck Institute for Polymer Research, Ackermannweg 10, 55128, Mainz, Germany.ORCID 0000-0001-6851-8453
Carsten SachseErnst Ruska-Centre for Microscopy and Spectroscopy with Electrons (ER-C-3): Structural Biology, Jülich, Germany. c.sachse@fz-juelich.de.ORCID 0000-0002-1168-5143
Dirk SchneiderDepartment of Chemistry, Biochemistry, Johannes Gutenberg University Mainz, Mainz, Germany. Dirk.Schneider@uni-mainz.de.ORCID 0000-0003-4517-6387
Johannes Gutenberg University Mainz · DEMax Planck Institute for Polymer Research · DEAarhus University · DKErnst Ruska Centre · DEForschungszentrum Jülich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

SynechocystisBacterial ProteinsDynaminsEukaryotaEukaryotic CellsGTP PhosphohydrolasesThylakoidsBacterial ProteinsDynaminsGTP Phosphohydrolases

Identifiers

PMID37059718
PMCPMC10104851
OpenAlexW4365503926

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.