Evidence map›Paper›PMID 23940054›Full record

ArticleThe Journal of biological chemistry2013

Control by potassium of the size distribution of Escherichia coli FtsZ polymers is independent of GTPase activity.

Rubén Ahijado-Guzmán, Carlos Alfonso, Belén Reija, Estefanía Salvarelli, Jesús Mingorance, Silvia Zorrilla, Begoña Monterroso, Germán Rivas

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. 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 at 5 institutions in 1 country.

Rubén Ahijado-GuzmánCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), 28040 Madrid.
Carlos AlfonsoCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), 28040 Madrid.
Belén ReijaInstituto de Química-Física Rocasolano, CSIC, 28006 Madrid.
Estefanía SalvarelliServicio de Microbiología, Hospital Universitario La Paz, IdiPAZ, 28046 Madrid; Biomol Informatics SL, Cantoblanco, 28049 Madrid, Spain.
Jesús MingoranceServicio de Microbiología, Hospital Universitario La Paz, IdiPAZ, 28046 Madrid.
Silvia ZorrillaInstituto de Química-Física Rocasolano, CSIC, 28006 Madrid.
Begoña MonterrosoCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), 28040 Madrid. Electronic address: monterroso@cib.csic.es.
Germán RivasCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), 28040 Madrid. Electronic address: grivas@cib.csic.es.
Centro de Investigaciones Biológicas Margarita Salas · ESInstituto de Química Física Blas Cabrera · ESBiomol Informatics (Spain) · ESConsejo Superior de Investigaciones Científicas · ESHospital Universitario La Paz · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The influence of potassium content (at neutral pH and millimolar Mg(2+)) on the size distribution of FtsZ polymers formed in the presence of constantly replenished GTP under steady-state conditions was studied by a combination of biophysical methods. The size of the GTP-FtsZ polymers decreased with lower potassium concentration, in contrast with the increase in the mass of the GDP-FtsZ oligomers, whereas no effect was observed on FtsZ GTPase activity and critical concentration of polymerization. Remarkably, the concerted formation of a narrow size distribution of GTP-FtsZ polymers previously observed at high salt concentration was maintained in all KCl concentrations tested. Polymers induced with guanosine 5'-(α,β-methylene)triphosphate, a slowly hydrolyzable analog of GTP, became larger and polydisperse as the potassium concentration was decreased. Our results suggest that the potassium dependence of the GTP-FtsZ polymer size may be related to changes in the subunit turnover rate that are independent of the GTP hydrolysis rate. The formation of a narrow size distribution of FtsZ polymers under very different solution conditions indicates that it is an inherent feature of FtsZ, not observed in other filament-forming proteins, with potential implications in the structural organization of the functional Z-ring.

Indexed as

Bacterial ProteinsCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsGTP PhosphohydrolasesGuanosine TriphosphatePotassiumProtein MultimerizationProtein Structure, QuaternaryBacterial ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsZ protein, BacteriaGTP PhosphohydrolasesGuanosine TriphosphatePotassiumBiophysicsCell DivisionGTPaseProtein AssemblyProtein-Protein Interactions

Identifiers

PMID23940054
PMCPMC3779730
OpenAlexW2111777358

What OpenQuestion holds

Textmetadata
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.