Evidence map›Paper›PMID 25433025›Full record

ArticleThe Journal of biological chemistry2015

Identification, characterization, and structure analysis of the cyclic di-AMP-binding PII-like signal transduction protein DarA.

Jan Gundlach, Achim Dickmanns, Kathrin Schröder-Tittmann, Piotr Neumann, Jan Kaesler, Jan Kampf, Christina Herzberg, Elke Hammer, Frank Schwede, Volkhard Kaever and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

51 citing papers in PubMed, 83 citations in OpenAlex.

  1. A c-di-AMP-controlled glutamine synthesis pathway promotes persistence ofbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. The role ofJournal of bacteriology · 2024
    Article
  7. Article
  8. Bacterial cell volume regulation and the importance of cyclic di-AMP.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. The World of Cyclic Dinucleotides in Bacterial Behavior.Molecules (Basel, Switzerland) · 2020
    Review
  20. Review
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

13 authors at 6 institutions in 3 countries.

Jan GundlachFrom the Departments of General Microbiology.
Achim DickmannsMolecular Structural Biology, and.
Kathrin Schröder-TittmannMolecular Enzymology, Georg August University Göttingen, 37077 Göttingen, Germany.
Piotr NeumannMolecular Structural Biology, and.
Jan KaeslerMolecular Structural Biology, and.
Jan KampfFrom the Departments of General Microbiology.
Christina HerzbergFrom the Departments of General Microbiology.
Elke HammerDepartment of Functional Genomics, Interfaculty Institute for Genetics and Functional Genomics, University Medicine Greifswald, 17487 Greifswald, Germany.
Frank SchwedeBIOLOG Life Science Institute, 28199 Bremen, Germany, and.
Volkhard KaeverResearch Core Unit Metabolomics, Hannover Medical School, 30625 Hannover, Germany.
Kai TittmannMolecular Enzymology, Georg August University Göttingen, 37077 Göttingen, Germany.
Jörg StülkeFrom the Departments of General Microbiology, jstuelk@gwdg.de.
Ralf FicnerMolecular Structural Biology, and rficner@uni-goettingen.de.
General Department of Preventive Medicine · VNInstitute of Structural and Molecular Biology · GBUniversity of Göttingen · DEBiolog Life Science Institute · DEMedizinische Hochschule Hannover · DEUniversitätsmedizin Greifswald · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cyclic dimeric AMP nucleotide c-di-AMP is an essential second messenger in Bacillus subtilis. We have identified the protein DarA as one of the prominent c-di-AMP receptors in B. subtilis. Crystal structure analysis shows that DarA is highly homologous to PII signal transducer proteins. In contrast to PII proteins, the functionally important B- and T-loops are swapped with respect to their size. DarA is a homotrimer that binds three molecules of c-di-AMP, each in a pocket located between two subunits. We demonstrate that DarA is capable to bind c-di-AMP and with lower affinity cyclic GMP-AMP (3'3'-cGAMP) but not c-di-GMP or 2'3'-cGAMP. Consistently the crystal structure shows that within the ligand-binding pocket only one adenine is highly specifically recognized, whereas the pocket for the other adenine appears to be promiscuous. Comparison with a homologous ligand-free DarA structure reveals that c-di-AMP binding is accompanied by conformational changes of both the fold and the position of the B-loop in DarA.

Indexed as

Bacillus subtilisBacterial ProteinsCrystallography, X-RayDinucleoside PhosphatesProtein Structure, SecondaryProtein Structure, TertiarySignal TransductionBacterial Proteinscyclic diadenosine phosphateDinucleoside PhosphatesBacterial Signal TransductionCrystal StructureCyclic Diadenosine Monophosphate (c-di-AMP)Cyclic Di-GMP (c-di-GMP)Isothermal Titration Calorimetry (ITC)

Identifiers

PMID25433025
PMCPMC4317042
OpenAlexW2053756731

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.