Evidence map›Paper›PMID 15569922›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Single-cell FRET imaging of phosphatase activity in the Escherichia coli chemotaxis system.

Ady Vaknin, Howard C Berg

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

54 citing papers in PubMed, 106 citations in OpenAlex.

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  5. Signal integration in chemoreceptor complexes.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  19. Bacterial protein networks: properties and functions.Nature reviews. Microbiology · 2015
    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

2 authors at 1 institution in 1 country.

Ady VakninDepartment of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.
Howard C Berg
Harvard University · US

Funding

SENSORY TRANSDUCTION IN BACTERIAL CHEMOTAXISR01AI016478 · NIAID · HARVARD UNIVERSITY · PI BERG, HOWARD C · 1985 to 2019
$14.1M
SENSORY TRANSDUCTION IN BACTERIAL CHEMOTAXISR37AI016478 · NIAID · HARVARD UNIVERSITY · PI BERG, HOWARD C · 1990 to 1999
–
NIAID NIH HHS AI16478NIAID NIH HHS R01 AI016478NIAID NIH HHS R37 AI016478
6 · The paper itself

Abstract

Two-component signaling systems, in which a receptor-coupled kinase is used to control the phosphorylation level of a response regulator, are commonly used in bacteria to sense their environment. In the chemotaxis system of Escherichia coli, the receptors, and thus the kinase, are clustered on the inner cell membrane. The phosphatase of this system also is recruited to receptor clusters, but the reason for this association is not clear. By using FRET imaging of single cells, we show that in vivo the phosphatase activity is substantially larger at the cluster, indicating that the signaling source (the kinase) and the signaling sink (the phosphatase) tend to be located at the same place in the cell. When this association is disrupted, a gradient in the concentration of the phosphorylated response regulator appears, and the chemotactic response is degraded. Such colocalization is inevitable in systems in which the activity of the kinase and the phosphatase are produced by the same enzyme. Evidently, this design enables a more rapid and spatially uniform response.

Indexed as

ChemotaxisBacterial ProteinsDiagnostic ImagingEscherichia coliEscherichia coli ProteinsFluorescence Resonance Energy TransferMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsPhosphoric Monoester HydrolasesPhosphotransferasesProtein BindingSignal TransductionBacterial ProteinsEscherichia coli ProteinsMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsPhosphoric Monoester HydrolasesPhosphotransferases

Identifiers

PMID15569922
PMCPMC535373
OpenAlexW2038541110

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.