Evidence map›Paper›PMID 23333741›Full record

ArticleJournal of molecular biology2013

Helix bundle loops determine whether histidine kinases autophosphorylate in cis or in trans.

Orr Ashenberg, Amy E Keating, Michael T Laub

Open access · bronzeAbstract read
In one paragraph

Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

38 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Chemical Reaction Models in Synthetic Promoter Design in Bacteria.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  6. A Model of the Full-Length Cytokinin Receptor: New Insights and Prospects.International journal of molecular sciences · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Hybrid histidine kinase activation by cyclic di-GMP-mediated domain liberation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Review
  13. Signal transduction in photoreceptor histidine kinases.Protein science : a publication of the Protein Society · 2019
    Review
  14. Article
  15. Control of theEcoSal Plus · 2019
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  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

3 authors at 1 institution in 1 country.

Orr AshenbergDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Amy E Keating
Michael T Laub
Massachusetts Institute of Technology · US

Funding

Analysis and Design of Coiled Coil PartneringR01GM067681 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KEATING, AMY E · 2004 to 2012
$2.9M
Howard Hughes Medical InstituteNIGMS NIH HHS GM067681NIGMS NIH HHS R01 GM067681
6 · The paper itself

Abstract

Bacteria frequently use two-component signal transduction pathways to sense and respond to environmental and intracellular stimuli. Upon receipt of a stimulus, a homodimeric sensor histidine kinase autophosphorylates and then transfers its phosphoryl group to a cognate response regulator. The autophosphorylation of histidine kinases has been reported to occur both in cis and in trans, but the molecular determinants dictating which mechanism is employed are unknown. Based on structural considerations, one model posits that the handedness of a loop at the base of the helical dimerization domain plays a critical role. Here, we tested this model by replacing the loop from Escherichia coli EnvZ, which autophosphorylates in trans, with the loop from three PhoR orthologs that autophosphorylate in cis. These chimeric kinases autophosphorylated in cis, indicating that this small loop is sufficient to determine autophosphorylation mechanism. Further, we report that the mechanism of autophosphorylation is conserved in orthologous sets of histidine kinases despite highly dissimilar loop sequences. These findings suggest that histidine kinases are under selective pressure to maintain their mode of autophosphorylation, but they can do so with a wide range of sequences.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsBacterial ProteinsElectrophoresis, Polyacrylamide GelEscherichia coliEscherichia coli ProteinsFluorescence Resonance Energy TransferHistidine KinaseKineticsLuminescent ProteinsModels, MolecularMolecular Sequence DataMultienzyme ComplexesMutationPhosphorylationProtein ConformationBacterial Outer Membrane ProteinsBacterial ProteinsenvZ protein, E coliEscherichia coli ProteinsHistidine KinaseLuminescent ProteinsMultienzyme ComplexesPhoR protein, BacteriaProtein Kinases

Identifiers

PMID23333741
PMCPMC3636764
OpenAlexW2085915112

What OpenQuestion holds

Textmetadata
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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.