Evidence map›Paper›PMID 38987236›Full record

ArticleNature communications2024

Polar confinement of a macromolecular machine by an SRP-type GTPase.

Anita Dornes, Lisa Marie Schmidt, Christopher-Nils Mais, John C Hook, Jan Pané-Farré, Dieter Kressler, Kai Thormann, Gert Bange

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. The polar landscape of bacterial pathogens and predators.Current opinion in microbiology · 2026
    Review
  2. Article
  3. Review
  4. The ancient E-ring in bacterial flagellar motors.FEMS microbiology reviews · 2026
    Review
  5. Article
  6. Article
  7. 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

8 authors.

Anita Dornes *Philipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, Hans-Meerwein-Strasse 6, C07, 35043, Marburg, Germany.ORCID 0000-0002-1060-3636
Lisa Marie Schmidt *Justus-Liebig-Universität, Department of Microbiology and Molecular Biology, Heinrich-Buff-Ring 26, 35392, Giessen, Germany.
Christopher-Nils MaisPhilipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, Hans-Meerwein-Strasse 6, C07, 35043, Marburg, Germany.
John C HookJustus-Liebig-Universität, Department of Microbiology and Molecular Biology, Heinrich-Buff-Ring 26, 35392, Giessen, Germany.
Jan Pané-FarréPhilipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, Hans-Meerwein-Strasse 6, C07, 35043, Marburg, Germany.ORCID 0000-0003-2723-2568
Dieter KresslerUniversity of Fribourg, Department of Biology, Chemin du Musée 10, 1700, Fribourg, Switzerland.ORCID 0000-0003-4855-3563
Kai ThormannJustus-Liebig-Universität, Department of Microbiology and Molecular Biology, Heinrich-Buff-Ring 26, 35392, Giessen, Germany. kai.thormann@mikro.bio.uni-giessen.de.ORCID 0000-0001-7292-4884
Gert BangePhilipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, Hans-Meerwein-Strasse 6, C07, 35043, Marburg, Germany. gert.bange@synmikro.uni-marburg.de.ORCID 0000-0002-7826-0932

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 495924434
6 · The paper itself

Abstract

The basal structure of the bacterial flagellum includes a membrane embedded MS-ring (formed by multiple copies of FliF) and a cytoplasmic C-ring (composed of proteins FliG, FliM and FliN). The SRP-type GTPase FlhF is required for directing the initial flagellar protein FliF to the cell pole, but the mechanisms are unclear. Here, we show that FlhF anchors developing flagellar structures to the polar landmark protein HubP/FimV, thereby restricting their formation to the cell pole. Specifically, the GTPase domain of FlhF interacts with HubP, while a structured domain at the N-terminus of FlhF binds to FliG. FlhF-bound FliG subsequently engages with the MS-ring protein FliF. Thus, the interaction of FlhF with HubP and FliG recruits a FliF-FliG complex to the cell pole. In addition, the modulation of FlhF activity by the MinD-type ATPase FlhG controls the interaction of FliG with FliM-FliN, thereby regulating the progression of flagellar assembly at the pole.

Indexed as

Bacterial ProteinsFlagellaGTP PhosphohydrolasesMembrane ProteinsMonomeric GTP-Binding ProteinsProtein BindingSignal Recognition ParticleBacterial ProteinsflhF protein, BacteriaFlif protein, BacteriaFlig protein, BacteriaGTP PhosphohydrolasesMembrane ProteinsMonomeric GTP-Binding ProteinsSignal Recognition Particle

Identifiers

PMID38987236
PMCPMC11236974

What OpenQuestion holds

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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.