Evidence map›Paper›PMID 28872847›Full record

ArticleBiochemistry2017

His-Tag-Mediated Dimerization of Chemoreceptors Leads to Assembly of Functional Nanoarrays.

Elizabeth R Haglin, Wen Yang, Ariane Briegel, Lynmarie K Thompson

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  9. Article
  10. Carbon-nitrogen REDOR to identify ms-timescale mobility in proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019
    Article
  11. Baseplate variability ofProceedings of the National Academy of Sciences of the United States of America · 2018
    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

4 authors at 2 institutions in 2 countries.

Elizabeth R Haglin
Wen YangDepartment of Biology, Leiden University , 2333 Leiden, The Netherlands.
Ariane BriegelDepartment of Biology, Leiden University , 2333 Leiden, The Netherlands.
Lynmarie K ThompsonORCID 0000-0002-9447-6776
Leiden University · NLUniversity of Massachusetts Amherst · US

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
Assembly and Function of Bacterial Chemotaxis Receptor Signaling ComplexesR01GM085288 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 2010 to 2013
$1.2M
NIGMS NIH HHS R01 GM085288NIGMS NIH HHS T32 GM008515
6 · The paper itself

Abstract

Transmembrane chemotaxis receptors are found in bacteria in extended hexagonal arrays stabilized by the membrane and by cytosolic binding partners, the kinase CheA and coupling protein CheW. Models of array architecture and assembly propose receptors cluster into trimers of dimers that associate with one CheA dimer and two CheW monomers to form the minimal "core unit" necessary for signal transduction. Reconstructing in vitro chemoreceptor ternary complexes that are homogeneous and functional and exhibit native architecture remains a challenge. Here we report that His-tag-mediated receptor dimerization with divalent metals is sufficient to drive assembly of nativelike functional arrays of a receptor cytoplasmic fragment. Our results indicate receptor dimerization initiates assembly and precedes formation of ternary complexes with partial kinase activity. Restoration of maximal kinase activity coincides with a shift to larger complexes, suggesting that kinase activity depends on interactions beyond the core unit. We hypothesize that achieving maximal activity requires building core units into hexagons and/or coalescing hexagons into the extended lattice. Overall, the minimally perturbing His-tag-mediated dimerization leads to assembly of chemoreceptor arrays with native architecture and thus serves as a powerful tool for studying the assembly and mechanism of this complex and other multiprotein complexes.

Indexed as

Protein MultimerizationBacterial ProteinsChemotaxisEscherichia coli ProteinsHistidineHistidine KinaseMethyl-Accepting Chemotaxis ProteinsModels, MolecularMultiprotein ComplexesOligopeptidesProtein BindingReceptors, Cell SurfaceSignal TransductionBacterial ProteinscheA protein, E coliCheW protein, E coliEscherichia coli ProteinsHis-His-His-His-His-HisHistidineHistidine KinaseMethyl-Accepting Chemotaxis ProteinsMultiprotein ComplexesOligopeptidesReceptors, Cell Surface

Identifiers

PMID28872847
PMCPMC5678893
OpenAlexW2751723555

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.