Evidence map›Paper›PMID 22908230›Full record

ArticleThe Journal of biological chemistry2012

Microtubule-like properties of the bacterial actin homolog ParM-R1.

David Popp, Akihiro Narita, Lin Jie Lee, Mårten Larsson, Robert C Robinson

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. 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

5 authors.

David PoppInstitute of Molecular and Cell Biology, Proteos, 61 Biopolis Drive, 138673, Singapore. dpopp@imcb.a-star.edu.sg
Akihiro Narita
Lin Jie Lee
Mårten Larsson
Robert C Robinson

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In preparation for mammalian cell division, microtubules repeatedly probe the cytoplasm to capture chromosomes and assemble the mitotic spindle. Critical features of this microtubule system are the formation of radial arrays centered at the centrosomes and dynamic instability, leading to persistent cycles of polymerization and depolymerization. Here, we show that actin homolog, ParM-R1 that drives segregation of the R1 multidrug resistance plasmid from Escherichia coli, can also self-organize in vitro into asters, which resemble astral microtubules. ParM-R1 asters grow from centrosome-like structures consisting of interconnected nodes related by a pseudo 8-fold symmetry. In addition, we show that ParM-R1 is able to perform persistent microtubule-like oscillations of assembly and disassembly. In vitro, a whole population of ParM-R1 filaments is synchronized between phases of growth and shrinkage, leading to prolonged synchronous oscillations even at physiological ParM-R1 concentrations. These results imply that the selection pressure to reliably segregate DNA during cell division has led to common mechanisms within diverse segregation machineries.

Indexed as

Escherichia coliActinsAdenosine TriphosphateAmino Acid SubstitutionEscherichia coli ProteinsFourier AnalysisGuanosine TriphosphateHydrolysisLightMicrotubulesMutagenesis, Site-DirectedProtein MultimerizationProtein Structure, QuaternaryScattering, RadiationActinsAdenosine TriphosphateEscherichia coli ProteinsGuanosine TriphosphateParM protein, E coli

Identifiers

PMID22908230
PMCPMC3481308

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.