Evidence map›Paper›PMID 21858888›Full record

ArticleProtein science : a publication of the Protein Society2011

Direct evidence that the carboxyl-terminal sequence of a bacterial chemoreceptor is an unstructured linker and enzyme tether.

Nicholas L Bartelli, Gerald L Hazelbauer

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. A chemoreceptor conformational equilibrium controlled by signaling inputs.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Evidence for Pentapeptide-Dependent and Independent CheB Methylesterases.International journal of molecular sciences · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Conformational shifts in a chemoreceptor helical hairpin control kinase signaling inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Bacterial chemoreceptor dynamics correlate with activity state and are coupled over long distances.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. Bacterial chemoreceptors and chemoeffectors.Cellular and molecular life sciences : CMLS · 2015
    Review
  20. 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

2 authors at 1 institution in 1 country.

Nicholas L BartelliDepartment of Biochemistry, 117 Schweitzer Hall, University of Missouri, Columbia, Missouri 65211, USA.
Gerald L Hazelbauer
University of Missouri · US

Funding

MOLECULAR STUDIES OF CHEMORECEPTIONR01GM029963 · NIGMS · WASHINGTON STATE UNIVERSITY · PI HAZELBAUER, GERALD L. · 1985 to 2010
$4.2M
NIGMS NIH HHS GM29963NIGMS NIH HHS R01 GM029963
6 · The paper itself

Abstract

Sensory adaptation in bacterial chemotaxis involves reversible methylation of specific glutamyl residues on chemoreceptors. The reactions are catalyzed by a dedicated methyltransferase and dedicated methylesterase. In Escherichia coli and related organisms, control of these enzymes includes an evolutionarily recent addition of interaction with a pentapeptide activator located at the carboxyl terminus of the receptor polypeptide chain. Effective enzyme activation requires not only the pentapeptide but also a segment of the receptor polypeptide chain between that sequence and the coiled-coil body of the chemoreceptor. This segment has features consistent with a role as a flexible and presumably unstructured linker and enzyme tether, but there has been no direct information about its structure. We used site-directed spin labeling and electron paramagnetic resonance spectroscopy to characterize structural features of the carboxyl-terminal 40 residues of E. coli chemoreceptor Tar. Beginning ∼ 35 residues from the carboxyl terminus and continuing to the end of the protein, spectra of spin-labeled Tar embedded in native membranes or in reconstituted proteoliposomes, exhibited mobilities characteristic of unstructured, disordered segments. Binding of methyltransferase substantially reduced mobility for positions in or near the pentapeptide but mobility for the linker sequence remained high, being only modestly reduced in a gradient of decreasing effects for 10-15 residues, a pattern consistent with the linker providing a flexible arm that would allow enzyme diffusion within defined limits. Thus, our data identify that the carboxyl-terminal linker between the receptor body and the pentapeptide is an unstructured, disordered segment that can serve as a flexible arm and enzyme tether.

Indexed as

ChemotaxisAmino Acid SequenceCell MembraneElectron Spin Resonance SpectroscopyEscherichia coliEscherichia coli ProteinsMethyltransferasesMolecular Sequence DataProtein ConformationProteolipidsReceptors, Cell SurfaceSequence Analysis, ProteinSpin LabelsEscherichia coli ProteinsMethyltransferasesProteolipidsproteoliposomesReceptors, Cell SurfaceSpin LabelsTar protein, E coli

Identifiers

PMID21858888
PMCPMC3267950
OpenAlexW2038828561

What OpenQuestion holds

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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.