Evidence map›Paper›PMID 29290041›Full record

ArticleProtoplasma2018

Oligomeric states in sodium ion-dependent regulation of cyanobacterial histidine kinase-2.

Iskander M Ibrahim, Liang Wang, Sujith Puthiyaveetil, Norbert Krauß, Jon Nield, John F Allen

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protoplasma, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 42% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

6 authors at 4 institutions in 3 countries.

Iskander M IbrahimDepartment of Biochemistry and Purdue Center for Plant Biology, Purdue University, West Lafayette, IN, USA.
Liang WangSchool of Biological and Chemical Sciences, Queen Mary University of London, London, UK.
Sujith PuthiyaveetilDepartment of Biochemistry and Purdue Center for Plant Biology, Purdue University, West Lafayette, IN, USA.
Norbert KraußBotanisches Institut, Karlsruher Institut für Technologie, Karlsruhe, Germany.
Jon NieldSchool of Biological and Chemical Sciences, Queen Mary University of London, London, UK.
John F AllenResearch Department of Genetics, Evolution and Environment, University College London, London, UK. j.f.allen@ucl.ac.uk.
Purdue University West Lafayette · USQueen Mary University of London · GBKarlsruhe Institute of Technology · DEUniversity College London · GB

Funding

Japan Science and Technology Corporation JPMJCR13M4Leverhulme Trust EM-2015-068Leverhulme Trust (GB) F/07 476/AQ
6 · The paper itself

Abstract

Two-component signal transduction systems (TCSs) consist of sensor histidine kinases and response regulators. TCSs mediate adaptation to environmental changes in bacteria, plants, fungi and protists. Histidine kinase 2 (Hik2) is a sensor histidine kinase found in all known cyanobacteria and as chloroplast sensor kinase in eukaryotic algae and plants. Sodium ions have been shown to inhibit the autophosphorylation activity of Hik2 that precedes phosphoryl transfer to response regulators, but the mechanism of inhibition has not been determined. We report on the mechanism of Hik2 activation and inactivation probed by chemical cross-linking and size exclusion chromatography together with direct visualisation of the kinase using negative-stain transmission electron microscopy of single particles. We show that the functional form of Hik2 is a higher-order oligomer such as a hexamer or octamer. Increased NaCl concentration converts the active hexamer into an inactive tetramer. The action of NaCl appears to be confined to the Hik2 kinase domain.

Indexed as

Protein MultimerizationChromatography, GelCross-Linking ReagentsCyanobacteriaHistidine KinaseIonsNegative StainingProtein DomainsRecombinant ProteinsSodiumSodium ChlorideCross-Linking ReagentsHistidine KinaseIonsRecombinant ProteinsSodiumSodium ChlorideOligomerisationProtein phosphorylationSensor histidine kinaseSingle-particle electron microscopySize-exclusion chromatographyTranscriptional regulationTwo-component regulatory system

Identifiers

PMID29290041
PMCPMC5904244
OpenAlexW2950072215

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.