Evidence map›Paper›PMID 27074767›Full record

ReviewCurrent genetics2016

Replenishing the cyclic-di-AMP pool: regulation of diadenylate cyclase activity in bacteria.

Thi Huong Pham, Zhao-Xun Liang, Esteban Marcellin, Mark S Turner

Abstract readReview
PubMed Publisher
In one paragraph

Review in Current genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Regulation of potassium homeostasis inFrontiers in microbiology · 2026
    Article
  3. Staying in the loop to make ends meet: roles and regulation of GlmR inbioRxiv : the preprint server for biology · 2025
    Article
  4. Inactivation of KhpB (EloR/Jag) inApplied and environmental microbiology · 2025
    Article
  5. Competence Regulation inCurrent medicinal chemistry · 2025
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. IPA-3: An Inhibitor of Diadenylate Cyclase ofAntibiotics (Basel, Switzerland) · 2022
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. The KupA and KupB Proteins ofJournal of bacteriology · 2019
    Article
  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

4 authors at 3 institutions in 2 countries.

Thi Huong PhamSchool of Agriculture and Food Sciences, University of Queensland, Brisbane, QLD, Australia.
Zhao-Xun LiangSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Esteban MarcellinAustralian Institute for Bioengineering and Nanotechnology, University of Queensland, Brisbane, QLD, Australia.
Mark S TurnerSchool of Agriculture and Food Sciences, University of Queensland, Brisbane, QLD, Australia. m.turner2@uq.edu.au.
University of Queensland · AUAgriculture and Food · AUNanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria can sense environmental cues and alter their physiology accordingly through the use of signal transduction pathways involving second messenger nucleotides. One broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Whilst extracellular stimuli regulating c-di-AMP levels in bacteria are poorly understood, recent work has identified effector proteins which directly interact and alter the activity of DACs. These include the membrane bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the membrane bound CdaA DAC and the recombination protein RadA which binds directly to the DNA binding DisA DAC. The genes encoding these multiprotein complexes are co-localised in many bacteria providing further support for their functional connection. The roles of GlmM in peptidoglycan synthesis and RadA in Holliday junction intermediate processing suggest that c-di-AMP synthesis by DACs will be responsive to these cellular activities. In addition to these modulatory interactions, permanent dysregulation of DAC activity due to suppressor mutations can occur during selection to overcome growth defects, rapid cell lysis and osmosensitivity. DACs have also been investigated as targets for the development of new antibiotics and several small compound inhibitors have recently been identified. This review aims to provide an overview of how c-di-AMP synthesis by DACs can be regulated.

Indexed as

BacteriaBacterial ProteinsDinucleoside PhosphatesEnzyme InhibitorsGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicMutationPhosphorus-Oxygen LyasesProtein BindingRepressor ProteinsSignal TransductionBacterial Proteinscyclic diadenosine phosphateDinucleoside PhosphatesEnzyme InhibitorsPhosphorus-Oxygen LyasesRepressor ProteinsCyclic-di-AMPDiadenylate cyclaseDNAPeptidoglycanRegulation

Identifiers

PMID27074767
OpenAlexW2339816615

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.