Evidence map›Paper›PMID 39019872›Full record

ArticleNature communications2024

Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule.

Chuan Qin, Leonie G Graf, Kilian Striska, Markus Janetzky, Norman Geist, Robin Specht, Sabrina Schulze, Gottfried J Palm, Britta Girbardt, Babett Dörre and 6 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
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  3. Article
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  5. Article
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  7. Review
  8. Staying in the loop to make ends meet: roles and regulation of GlmR inbioRxiv : the preprint server for biology · 2025
    Article
  9. Csn5 Depletion Reverses Mitochondrial Defects in GCN5-NullInternational journal of molecular sciences · 2025
    Article
  10. Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Intracellular acetyl phosphate modulatesActa biochimica et biophysica Sinica · 2025
    Article
  13. Article
  14. Fatty acid metabolism and the oxidative stress response support bacterial predation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. 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

16 authors.

Chuan QinDepartment of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Leonie G GrafDepartment of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Kilian StriskaDepartment of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Markus JanetzkyDepartment of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Norman GeistDepartment of Biophysical Chemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.ORCID 0000-0001-9671-8882
Robin SpechtDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.ORCID 0009-0006-2701-6776
Sabrina SchulzeDepartment of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.ORCID 0000-0002-0122-5688
Gottfried J PalmDepartment of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.ORCID 0000-0003-0329-0413
Britta GirbardtDepartment of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Babett DörreDepartment of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Leona BerndtDepartment of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Stefan KemnitzDepartment for High Performance Computing, University Computing Center, University of Greifswald, 17489, Greifswald, Germany.
Mark DoerrDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.ORCID 0000-0003-3270-6895
Uwe T BornscheuerDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.ORCID 0000-0003-0685-2696
Mihaela DelceaDepartment of Biophysical Chemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.ORCID 0000-0002-0851-9072
Michael LammersDepartment of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany. michael.lammers@uni-greifswald.de.ORCID 0000-0003-4168-4640

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) LA2984-6/1
6 · The paper itself

Abstract

The AMP-forming acetyl-CoA synthetase is regulated by lysine acetylation both in bacteria and eukaryotes. However, the underlying mechanism is poorly understood. The Bacillus subtilis acetyltransferase AcuA and the AMP-forming acetyl-CoA synthetase AcsA form an AcuA•AcsA complex, dissociating upon lysine acetylation of AcsA by AcuA. Crystal structures of AcsA from Chloroflexota bacterium in the apo form and in complex with acetyl-adenosine-5'-monophosphate (acetyl-AMP) support the flexible C-terminal domain adopting different conformations. AlphaFold2 predictions suggest binding of AcuA stabilizes AcsA in an undescribed conformation. We show the AcuA•AcsA complex dissociates upon acetyl-coenzyme A (acetyl-CoA) dependent acetylation of AcsA by AcuA. We discover an intrinsic phosphotransacetylase activity enabling AcuA•AcsA generating acetyl-CoA from acetyl-phosphate (AcP) and coenzyme A (CoA) used by AcuA to acetylate and inactivate AcsA. Here, we provide mechanistic insights into the regulation of AMP-forming acetyl-CoA synthetases by lysine acetylation and discover an intrinsic phosphotransacetylase allowing modulation of its activity based on AcP and CoA levels.

Indexed as

Acetate-CoA LigaseAcetyl Coenzyme ABacillus subtilisBacterial ProteinsLysineAcetylationAdenosine MonophosphateCrystallography, X-RayModels, MolecularOrganophosphatesProtein BindingAcetate-CoA LigaseAcetyl Coenzyme Aacetyl phosphateAdenosine MonophosphateBacterial ProteinsLysineOrganophosphates

Identifiers

PMID39019872
PMCPMC11255334

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Registered trials

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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.