Evidence map›Paper›PMID 18427119›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Protein exchange dynamics at chemoreceptor clusters in Escherichia coli.

Sonja Schulmeister, Michaela Ruttorf, Sebastian Thiem, David Kentner, Dirk Lebiedz, Victor Sourjik

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed.

  1. Article
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  12. Single-molecule imaging of electroporated dye-labelled CheY in live Escherichia coli.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016
    Article
  13. Caulobacter PopZ forms an intrinsically disordered hub in organizing bacterial cell poles.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Article
  15. Bacterial protein networks: properties and functions.Nature reviews. Microbiology · 2015
    Review
  16. Article
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  19. Review
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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.

Sonja SchulmeisterZentrum für Molekulare Biologie and Interdisziplinäres Zentrum für Wissenschaftliches Rechnen, Universität Heidelberg, D-69120 Heidelberg, Germany.
Michaela Ruttorf
Sebastian Thiem
David Kentner
Dirk Lebiedz
Victor Sourjik

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signal processing in bacterial chemotaxis relies on large sensory complexes consisting of thousands of protein molecules. These clusters create a scaffold that increases the efficiency of pathway reactions and amplifies and integrates chemotactic signals. The cluster core in Escherichia coli comprises a ternary complex composed of receptors, kinase CheA, and adaptor protein CheW. All other chemotaxis proteins localize to clusters by binding either directly to receptors or to CheA. Here, we used fluorescence recovery after photobleaching (FRAP) to investigate the turnover of chemotaxis proteins at the cluster and their mobility in the cytoplasm. We found that cluster exchange kinetics were protein-specific and took place on several characteristic time scales that correspond to excitation, adaptation, and cell division, respectively. We further applied analytical and numerical data fitting to analyze intracellular protein diffusion and to estimate the rate constants of cluster equilibration in vivo. Our results indicate that the rates of protein turnover at the cluster have evolved to ensure optimal performance of the chemotaxis pathway.

Indexed as

Bacterial ProteinsChemoreceptor CellsChemotaxisDiffusionEscherichia coliEscherichia coli ProteinsFluorescence Recovery After PhotobleachingKineticsProtein BindingProtein TransportRecombinant Fusion ProteinsBacterial ProteinsEscherichia coli ProteinsRecombinant Fusion Proteins

Identifiers

PMID18427119
PMCPMC2359816

What OpenQuestion holds

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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.