Evidence map›Paper›PMID 26787847›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification.

Frédéric V Stanger, Björn M Burmann, Alexander Harms, Hugo Aragão, Adam Mazur, Timothy Sharpe, Christoph Dehio, Sebastian Hiller, Tilman Schirmer

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Inhibition of FicD-mediated AMPylation and deAMPylation by isoprenoid diphosphates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. AMPylation: key roles in biological regulation across prokaryotes and eukaryotes.Frontiers in cellular and infection microbiology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Prokaryote toxin-antitoxin modules: Complex regulation of an unclear function.Protein science : a publication of the Protein Society · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. A CaNature communications · 2019
    Article
  13. Article
  14. Review
  15. Review
  16. Fic Proteins ofFrontiers in microbiology · 2017
    Article
  17. Article
  18. Article
  19. 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

9 authors at 1 institution in 2 countries.

Frédéric V StangerFocal Area Structural Biology and Biophysics, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Focal Area Infection Biology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland;
Björn M BurmannFocal Area Structural Biology and Biophysics, Biozentrum, University of Basel, CH-4056 Basel, Switzerland;ORCID http://orcid.org/0000-0002-3135-7964
Alexander HarmsFocal Area Infection Biology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland;
Hugo AragãoFocal Area Structural Biology and Biophysics, Biozentrum, University of Basel, CH-4056 Basel, Switzerland;
Adam MazurResearch IT, Biozentrum, University of Basel, CH-4056 Basel, Switzerland;
Timothy SharpeBiophysics Facility, Biozentrum, University of Basel, CH-4056 Basel, Switzerland.
Christoph DehioFocal Area Infection Biology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; christoph.dehio@unibas.ch sebastian.hiller@unibas.ch tilman.schirmer@unibas.ch.
Sebastian HillerFocal Area Structural Biology and Biophysics, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; christoph.dehio@unibas.ch sebastian.hiller@unibas.ch tilman.schirmer@unibas.ch.ORCID http://orcid.org/0000-0002-6709-4684
Tilman SchirmerFocal Area Structural Biology and Biophysics, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; christoph.dehio@unibas.ch sebastian.hiller@unibas.ch tilman.schirmer@unibas.ch.
University of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Filamentation induced by cyclic AMP (FIC)-domain enzymes catalyze adenylylation or other posttranslational modifications of target proteins to control their function. Recently, we have shown that Fic enzymes are autoinhibited by an α-helix (αinh) that partly obstructs the active site. For the single-domain class III Fic proteins, the αinh is located at the C terminus and its deletion relieves autoinhibition. However, it has remained unclear how activation occurs naturally. Here, we show by structural, biophysical, and enzymatic analyses combined with in vivo data that the class III Fic protein NmFic from Neisseria meningitidis gets autoadenylylated in cis, thereby autonomously relieving autoinhibition and thus allowing subsequent adenylylation of its target, the DNA gyrase subunit GyrB. Furthermore, we show that NmFic activation is antagonized by tetramerization. The combination of autoadenylylation and tetramerization results in nonmonotonic concentration dependence of NmFic activity and a pronounced lag phase in the progress of target adenylylation. Bioinformatic analyses indicate that this elaborate dual-control mechanism is conserved throughout class III Fic proteins.

Indexed as

Bacterial ProteinsBiopolymersCyclic AMPDNA GyraseModels, MolecularNeisseria meningitidisNucleotidyltransferasesBacterial ProteinsBiopolymersCyclic AMPDNA GyraseNucleotidyltransferasesadenylylationAMPylationenzyme regulationmolecular timerposttranslational modification

Identifiers

PMID26787847
PMCPMC4747691
OpenAlexW2276745282

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.