Evidence map›Paper›PMID 31672986›Full record

ArticleNature communications2019

De novo synthesized Min proteins drive oscillatory liposome deformation and regulate FtsA-FtsZ cytoskeletal patterns.

Elisa Godino, Jonás Noguera López, David Foschepoth, Céline Cleij, Anne Doerr, Clara Ferrer Castellà, Christophe Danelon

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
10.0field-weighted citation impact, top 1% 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

41 citing papers in PubMed, 106 citations in OpenAlex.

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  14. SecYEG-mediated translocation in a model synthetic cell.Synthetic biology (Oxford, England) · 2024
    Article
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  20. Compartmentalized Cell-Free Expression Systems for Building Synthetic Cells.Advances in biochemical engineering/biotechnology · 2023
    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

7 authors at 1 institution in 1 country.

Elisa GodinoDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, van der Maasweg 9, 2629HZ, Delft, The Netherlands.
Jonás Noguera LópezDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, van der Maasweg 9, 2629HZ, Delft, The Netherlands.
David FoschepothDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, van der Maasweg 9, 2629HZ, Delft, The Netherlands.ORCID http://orcid.org/0000-0001-7116-7121
Céline CleijDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, van der Maasweg 9, 2629HZ, Delft, The Netherlands.ORCID http://orcid.org/0000-0001-6580-1106
Anne DoerrDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, van der Maasweg 9, 2629HZ, Delft, The Netherlands.
Clara Ferrer CastellàDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, van der Maasweg 9, 2629HZ, Delft, The Netherlands.
Christophe DanelonDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, van der Maasweg 9, 2629HZ, Delft, The Netherlands. c.j.a.danelon@tudelft.nl.
Delft University of Technology · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Min biochemical network regulates bacterial cell division and is a prototypical example of self-organizing molecular systems. Cell-free assays relying on purified proteins have shown that MinE and MinD self-organize into surface waves and oscillatory patterns. In the context of developing a synthetic cell from elementary biological modules, harnessing Min oscillations might allow us to implement higher-order cellular functions. To convey hereditary information, the Min system must be encoded in a DNA molecule that can be copied, transcribed, and translated. Here, the MinD and MinE proteins are synthesized de novo from their genes inside liposomes. Dynamic protein patterns and accompanying liposome shape deformation are observed. When integrated with the cytoskeletal proteins FtsA and FtsZ, the synthetic Min system is able to dynamically regulate FtsZ patterns. By enabling genetic control over Min protein self-organization and membrane remodeling, our methodology offers unique opportunities towards directed evolution of bacterial division processes in vitro.

Indexed as

Adenosine TriphosphatasesArtificial CellsBacterial ProteinsCell Cycle ProteinsCell DivisionCell-Free Nucleic AcidsCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsLipid BilayersLiposomesMembrane ProteinsAdenosine TriphosphatasesBacterial ProteinsCell Cycle ProteinsCell-Free Nucleic AcidsCytoskeletal ProteinsEscherichia coli ProteinsFtsA protein, E coliFtsZ protein, BacteriaLipid BilayersLiposomesMembrane ProteinsMinC protein, E coliMinD protein, E coliMinE protein, E coli

Identifiers

PMID31672986
PMCPMC6823393
OpenAlexW2982306254

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.