Evidence map›Paper›PMID 33581219›Full record

ArticleBiochimica et biophysica acta. Molecular cell research2021

Assembly of bacterial cell division protein FtsZ into dynamic biomolecular condensates.

Miguel Ángel Robles-Ramos, Silvia Zorrilla, Carlos Alfonso, William Margolin, Germán Rivas, Begoña Monterroso

Abstract read
In one paragraph

Article in Biochimica et biophysica acta. Molecular cell research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Glycerol-Driven Energy and Proteostasis Underpin Antibiotic Tolerance inbioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Protein oxidation in crowded environments.The Biochemical journal · 2026
    Review
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  18. Interactions between Phase-Separated Liquids and Membrane Surfaces.Applied sciences (Basel, Switzerland) · 2021
    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

6 authors.

Miguel Ángel Robles-RamosCentro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas (CSIC), 28040 Madrid, Spain.
Silvia ZorrillaCentro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas (CSIC), 28040 Madrid, Spain. Electronic address: silvia@cib.csic.es.
Carlos AlfonsoCentro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas (CSIC), 28040 Madrid, Spain.
William MargolinDepartment of Microbiology and Molecular Genetics, McGovern Medical School, University of Texas, Houston, TX 77030, USA.
Germán RivasCentro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas (CSIC), 28040 Madrid, Spain. Electronic address: grivas@cib.csic.es.
Begoña MonterrosoCentro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas (CSIC), 28040 Madrid, Spain. Electronic address: monterroso@cib.csic.es.

Funding

Mechanisms and Regulation of Cell Division in BacteriaR35GM131705 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI WILLIAM MARGOLIN · 2019 to 2026
$3.8M
NIGMS NIH HHS R35 GM131705
6 · The paper itself

Abstract

Biomolecular condensation through phase separation may be a novel mechanism to regulate bacterial processes, including cell division. Previous work revealed that FtsZ, a protein essential for cytokinesis in most bacteria, forms biomolecular condensates with SlmA, a protein that protects the chromosome from damage inflicted by the division machinery in Escherichia coli. The absence of condensates composed solely of FtsZ under the conditions used in that study suggested this mechanism was restricted to nucleoid occlusion by SlmA or to bacteria containing this protein. Here we report that FtsZ alone, under physiologically relevant conditions, can demix into condensates in bulk and when encapsulated in synthetic cell-like systems generated by microfluidics. Condensate assembly depends on FtsZ being in the GDP-bound state and on conditions mimicking the crowded environment of the cytoplasm that promote its oligomerization. Condensates are dynamic and reversibly convert into filaments upon GTP addition. Notably, FtsZ lacking its C-terminal disordered region, a structural element likely to favor biomolecular condensation, also forms condensates, albeit less efficiently. The inherent tendency of FtsZ to form condensates susceptible to modulation by physiological factors, including binding partners, suggests that such mechanisms may play a more general role in bacterial division than initially envisioned.

Indexed as

Bacterial ProteinsCytoplasmCytoskeletal ProteinsEscherichia coliGuanosine DiphosphateMicrofluidic Analytical TechniquesMicroscopy, FluorescenceNephelometry and TurbidimetryProtein DomainsProtein MultimerizationSequence DeletionBacterial ProteinsCytoskeletal ProteinsFtsZ protein, BacteriaGuanosine DiphosphateMacromolecular crowdingMembraneless compartmentsMicrofluidicsPhase separationSubcellular organization

Identifiers

PMID33581219
PMCPMC8529516

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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.