Evidence map›Paper›PMID 33172954›Full record

ArticleScience signaling2020

Engineered chemotaxis core signaling units indicate a constrained kinase-off state.

Alise R Muok, Teck Khiang Chua, Madhur Srivastava, Wen Yang, Zach Maschmann, Petr P Borbat, Jenna Chong, Sheng Zhang, Jack H Freed, Ariane Briegel and 1 more

Open access · greenAbstract read
In one paragraph

Article in Science signaling, 2020. 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
2.5field-weighted citation impact, top 10% 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, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. 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
  7. Article
  8. Small-angle X-ray scattering studies of enzymes.Current opinion in chemical biology · 2023
    Review
  9. Review
  10. Article
  11. 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

11 authors at 2 institutions in 3 countries.

Alise R MuokDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.ORCID 0000-0001-8695-3221
Teck Khiang ChuaDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.ORCID 0000-0001-6569-0813
Madhur SrivastavaDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.ORCID 0000-0002-2095-0412
Wen YangInstitute for Biology, Leiden University, Sylviusweg 72, 2333 BE Leiden, Netherlands.
Zach MaschmannDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.ORCID 0000-0002-7938-0792
Petr P BorbatDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Jenna ChongDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.ORCID 0000-0003-0898-1184
Sheng ZhangDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.ORCID 0000-0001-8206-1007
Jack H FreedDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.ORCID 0000-0003-4288-2585
Ariane BriegelInstitute for Biology, Leiden University, Sylviusweg 72, 2333 BE Leiden, Netherlands.ORCID 0000-0003-3733-3725
Brian R CraneDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA. bc69@cornell.edu.ORCID 0000-0001-8234-9991
Cornell University · USLeiden University · NL

Funding

Training and OutreachP30GM124166 · NIGMS · CORNELL UNIVERSITY · PI RICHARD A. CERIONE · 2019 to 2026
$28.3M
Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
TR&D 4 for ACERT, 2017-2021 funding periodP41GM103521 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2012 to 2021
$11.7M
Molecular Mechanisms of Signal Transduction Involving Light, Redox and Transmembrane ComplexesR35GM122535 · NIGMS · CORNELL UNIVERSITY · PI BRIAN R CRANE · 2017 to 2026
$7.1M
Electron Spin Relaxation in Model MembranesR01GM123779 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2017 to 2020
$2.1M
X/Q Band Pulsed ENDOR SpectrometerS10OD021543 · OD · CORNELL UNIVERSITY · PI FREED, JACK H · 2016 to 2016
$1.4M
Acquisition of a Hybrid Quadrupole Time of Flight LC-MS/MS System for the CornellS10OD017992 · OD · CORNELL UNIVERSITY · PI ZHANG, SHENG · 2014 to 2014
$600k
NIGMS NIH HHS P30 GM124166NIGMS NIH HHS P41 GM103485NIGMS NIH HHS P41 GM103521NIGMS NIH HHS R01 GM123779NIGMS NIH HHS R35 GM122535NIH HHS S10 OD017992NIH HHS S10 OD021543
6 · The paper itself

Abstract

Bacterial chemoreceptors, the histidine kinase CheA, and the coupling protein CheW form transmembrane molecular arrays with remarkable sensing properties. The receptors inhibit or stimulate CheA kinase activity depending on the presence of attractants or repellants, respectively. We engineered chemoreceptor cytoplasmic regions to assume a trimer of receptor dimers configuration that formed well-defined complexes with CheA and CheW and promoted a CheA kinase-off state. These mimics of core signaling units were assembled to homogeneity and investigated by site-directed spin-labeling with pulse-dipolar electron-spin resonance spectroscopy (PDS), small-angle x-ray scattering, targeted protein cross-linking, and cryo-electron microscopy. The kinase-off state was especially stable, had relatively low domain mobility, and associated the histidine substrate and docking domains with the kinase core, thus preventing catalytic activity. Together, these data provide an experimentally restrained model for the inhibited state of the core signaling unit and suggest that chemoreceptors indirectly sequester the kinase and substrate domains to limit histidine autophosphorylation.

Indexed as

ChemotaxisSignal TransductionEscherichia coliEscherichia coli ProteinsHistidine KinaseMethyl-Accepting Chemotaxis ProteinsMultiprotein ComplexesProtein Structure, QuaternarycheA protein, E coliCheW protein, E coliEscherichia coli ProteinsHistidine KinaseMethyl-Accepting Chemotaxis ProteinsMultiprotein Complexes

Identifiers

PMID33172954
PMCPMC7790435
OpenAlexW3103273573

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.