Evidence map›Paper›PMID 26251518›Full record

ArticleThe Journal of biological chemistry2015

The Protein Acetyltransferase PatZ from Escherichia coli Is Regulated by Autoacetylation-induced Oligomerization.

Teresa de Diego Puente, Julia Gallego-Jara, Sara Castaño-Cerezo, Vicente Bernal Sánchez, Vanesa Fernández Espín, José García de la Torre, Arturo Manjón Rubio, Manuel Cánovas Díaz

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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

21 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. 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
  3. Metabolic Engineering ofACS synthetic biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. An insight into the role of the N-terminal domain ofFrontiers in molecular biosciences · 2024
    Article
  9. An acetyltranferase moonlights as a regulator of the RNA binding repertoire of the RNA chaperone Hfq inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Protein Acetylation in Bacteria.Annual review of microbiology · 2019
    Review
  16. Article
  17. Review
  18. Review
  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

8 authors at 1 institution in 1 country.

Teresa de Diego PuenteFrom the Departments of Biochemistry and Molecular Biology and Immunology (B) and tdp@um.es.
Julia Gallego-JaraFrom the Departments of Biochemistry and Molecular Biology and Immunology (B) and.
Sara Castaño-CerezoFrom the Departments of Biochemistry and Molecular Biology and Immunology (B) and.
Vicente Bernal SánchezFrom the Departments of Biochemistry and Molecular Biology and Immunology (B) and.
Vanesa Fernández EspínPhysical Chemistry, Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum," P. O. Box 4021, Murcia E-30100, Spain.
José García de la TorrePhysical Chemistry, Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum," P. O. Box 4021, Murcia E-30100, Spain.
Arturo Manjón RubioFrom the Departments of Biochemistry and Molecular Biology and Immunology (B) and.
Manuel Cánovas DíazFrom the Departments of Biochemistry and Molecular Biology and Immunology (B) and.
Bipar · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine acetylation is an important post-translational modification in the metabolic regulation of both prokaryotes and eukaryotes. In Escherichia coli, PatZ (formerly YfiQ) is the only known acetyltransferase protein and is responsible for acetyl-CoA synthetase acetylation. In this study, we demonstrated PatZ-positive cooperativity in response to acetyl-CoA and the regulation of acetyl-CoA synthetase activity by the acetylation level. Furthermore, functional analysis of an E809A mutant showed that the conserved glutamate residue is not relevant for the PatZ catalytic mechanism. Biophysical studies demonstrated that PatZ is a stable tetramer in solution and is transformed to its octameric form by autoacetylation. Moreover, this modification is reversed by the sirtuin CobB. Finally, an in silico PatZ tetramerization model based on hydrophobic and electrostatic interactions is proposed and validated by three-dimensional hydrodynamic analysis. These data reveal, for the first time, the structural regulation of an acetyltransferase by autoacetylation in a prokaryotic organism.

Indexed as

Models, MolecularProtein MultimerizationAcetylationAcetyltransferasesAmino Acid SubstitutionAnimalsCoenzyme A LigasesEscherichia coliEscherichia coli ProteinsHumansMiceMutation, MissenseProtein Structure, QuaternarySirtuinsacetate-CoA ligase (ADP-forming)acetyl-CoA synthetase acetylase, E coliAcetyltransferasescobB protein, E ColiCoenzyme A LigasesEscherichia coli ProteinsSirtuinsacetyl-CoA synthetaseacetyl coenzyme A (acetyl-CoA)acetyltransferaseautoacetylationEscherichia coli (E. coli)lysine acetylationoligomerizationpost-translational modification (PTM)protein acetyltransferase (PatZ or YfiQ)

Identifiers

PMID26251518
PMCPMC4645606
OpenAlexW1922633863

What OpenQuestion holds

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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.