Evidence map›Paper›PMID 28622374›Full record

ArticlePloS one2017

Large-scale modulation of reconstituted Min protein patterns and gradients by defined mutations in MinE's membrane targeting sequence.

Simon Kretschmer, Katja Zieske, Petra Schwille

Abstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Engineering spatiotemporal organization and dynamics in synthetic cells.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2021
    Review
  5. Article
  6. C-terminal eYFP fusion impairsOpen biology · 2020
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Reverse and forward engineering of protein pattern formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Article
  13. Self-organization principles of intracellular pattern formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  14. The Min-protein oscillations inPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  15. MinE conformational switching confers robustness on self-organized Min protein patterns.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Review
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

3 authors.

Simon KretschmerDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Katja ZieskeDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Petra SchwilleDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0002-6106-4847

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The E. coli MinDE oscillator is a paradigm for protein self-organization and gradient formation. Previously, we reconstituted Min protein wave patterns on flat membranes as well as gradient-forming pole-to-pole oscillations in cell-shaped PDMS microcompartments. These oscillations appeared to require direct membrane interaction of the ATPase activating protein MinE. However, it remained unclear how exactly Min protein dynamics are regulated by MinE membrane binding. Here, we dissect the role of MinE's membrane targeting sequence (MTS) by reconstituting various MinE mutants in 2D and 3D geometries. We demonstrate that the MTS defines the lower limit of the concentration-dependent wavelength of Min protein patterns while restraining MinE's ability to stimulate MinD's ATPase activity. Strikingly, a markedly reduced length scale-obtainable even by single mutations-is associated with a rich variety of multistable dynamic modes in cell-shaped compartments. This dramatic remodeling in response to biochemical changes reveals a remarkable trade-off between robustness and versatility of the Min oscillator.

Indexed as

Adenosine TriphosphatasesCell Cycle ProteinsEscherichia coliEscherichia coli ProteinsMembrane MicrodomainsBiological ClocksMutationProtein BindingAdenosine TriphosphatasesCell Cycle ProteinsEscherichia coli ProteinsMinD protein, E coliMinE protein, E coli

Identifiers

PMID28622374
PMCPMC5473585

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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.