Evidence map›Paper›PMID 16163393›Full record

ArticleThe EMBO journal2005

A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis.

Janine Kirstein, Daniela Zühlke, Ulf Gerth, Kürşad Turgay, Michael Hecker

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

56 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structural insights into the regulation of protein-arginine kinase McsB by McsA.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Review
  6. Review
  7. Article
  8. Widespread Arginine Phosphorylation in Staphylococcus aureus.Molecular & cellular proteomics : MCP · 2022
    Article
  9. Update on the Protein Homeostasis Network inFrontiers in microbiology · 2022
    Review
  10. Article
  11. Article
  12. Xenogeneic modulation of the ClpCP protease ofThe Journal of biological chemistry · 2019
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. CtsR, the Master Regulator of Stress-Response inFrontiers in microbiology · 2018
    Article
  18. Functional Diversity of AAA+ Protease Complexes inFrontiers in molecular biosciences · 2017
    Review
  19. AAA+ Machines of Protein Destruction in Mycobacteria.Frontiers in molecular biosciences · 2017
    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

5 authors at 2 institutions in 1 country.

Janine KirsteinErnst Moritz Arndt Universität Greifswald, Institut für Molekulare Mikrobiologie, Greifswald, Germany. jkfu@zedat.fu-berlin.de
Daniela Zühlke
Ulf Gerth
Kürşad Turgay
Michael Hecker
Universität Greifswald · DEFreie Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The soil bacterium Bacillus subtilis possesses a fine-tuned and complex heat stress response system. The repressor CtsR, whose activity is regulated by its modulators McsA and McsB, controls the expression of the cellular protein quality control genes clpC, clpE and clpP. Here, we show that the interaction of McsA and McsB with CtsR results in the formation of a ternary complex that not only prevents the binding of CtsR to its target DNA, but also results in a subsequent phosphorylation of McsB, McsA and CtsR. We further demonstrate that McsB is a tyrosine kinase that needs McsA to become activated. ClpC inhibits the kinase activity of McsB, indicating a direct role in initiating CtsR-controlled heat shock response. Interestingly, the kinase domain of McsB is homologous to guanidino phosphotransferase domains originating from eukaryotic arginine and creatine kinases. Mutational analysis of key residues of the guanidino kinase domain demonstrated that McsB utilizes this domain to catalyze the tyrosine phosphorylation. McsB represents therefore a new kind of tyrosine kinase, driven by a guanidino phosphotransferase domain.

Indexed as

Gene Expression Regulation, EnzymologicModels, MolecularAdenosine TriphosphatasesAmino Acid SequenceBacillus subtilisBacterial ProteinsBlotting, WesternElectrophoresis, Polyacrylamide GelElectrophoretic Mobility Shift AssayHeat-Shock ProteinsHeat-Shock ResponseImmunoprecipitationMolecular Sequence DataPhosphorylationProtein KinasesRepressor ProteinsAdenosine TriphosphatasesBacterial ProteinsClpC protein, BacteriaClpE protein, bacteriaCtsR protein, bacteriaHeat-Shock ProteinsMcsA protein, Bacillus subtilisMcsB protein, Bacillus subtilisProtein KinasesRepressor Proteins

Identifiers

PMID16163393
PMCPMC1276163
OpenAlexW2134165623

What OpenQuestion holds

Textmetadata
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.