Evidence map›Paper›PMID 41730913›Full record

ArticleNature communications2026

A protein adaptor mediating Ap4A-dependent control of protein acetylation.

Liujuan Zheng, Megan K M Young, Wieland Steinchen, Zhiyong Guo, Ekaterina Jalomo-Khayrova, Bobby Xuanyu Liu, Fabiana Burchert, Patricia Bedrunka, Christopher-Nils Mais, Jan Pané-Farré and 8 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Loss of the ApJournal of bacteriology · 2026
    Article
  2. Article
  3. Molecular insights into the promiscuous ApThe Journal of biological chemistry · 2026
    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

18 authors.

Liujuan ZhengMax Planck Institute for Terrestrial Microbiology, Marburg, Germany.ORCID http://orcid.org/0009-0003-6716-5694
Megan K M YoungDepartment of Bacteriology, University of Wisconsin-Madison, Madison, WI, USA.
Wieland SteinchenMarburg University, Center for Synthetic Microbiology (SYNMIKRO) & Department of Chemistry, Marburg, Germany.
Zhiyong GuoState Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Key Laboratory of Industrial Biotechnology, School of Life Sciences, Hubei University, Wuhan, China.ORCID http://orcid.org/0009-0003-4334-2713
Ekaterina Jalomo-KhayrovaMarburg University, Center for Synthetic Microbiology (SYNMIKRO) & Department of Chemistry, Marburg, Germany.
Bobby Xuanyu LiuDepartment of Bacteriology, University of Wisconsin-Madison, Madison, WI, USA.
Fabiana BurchertMarburg University, Center for Synthetic Microbiology (SYNMIKRO) & Department of Chemistry, Marburg, Germany.ORCID http://orcid.org/0009-0000-2956-5409
Patricia BedrunkaMarburg University, Center for Synthetic Microbiology (SYNMIKRO) & Department of Chemistry, Marburg, Germany.ORCID http://orcid.org/0000-0002-9984-5518
Christopher-Nils MaisMarburg University, Center for Synthetic Microbiology (SYNMIKRO) & Department of Chemistry, Marburg, Germany.
Jan Pané-FarréMarburg University, Center for Synthetic Microbiology (SYNMIKRO) & Department of Chemistry, Marburg, Germany.
Mathias GirbigMax Planck Institute for Terrestrial Microbiology, Marburg, Germany.ORCID http://orcid.org/0000-0003-3442-5448
Uwe LinneMarburg University, Center for Synthetic Microbiology (SYNMIKRO) & Department of Chemistry, Marburg, Germany.ORCID http://orcid.org/0000-0002-1473-9063
Aude TrinquierDepartment of Bacteriology, University of Wisconsin-Madison, Madison, WI, USA.ORCID http://orcid.org/0000-0003-1188-2005
Aitao LiState Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Key Laboratory of Industrial Biotechnology, School of Life Sciences, Hubei University, Wuhan, China.ORCID http://orcid.org/0000-0001-6036-4058
Georg HochbergMax Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Johannes FreitagMarburg University, Center for Synthetic Microbiology (SYNMIKRO) & Department of Chemistry, Marburg, Germany.ORCID http://orcid.org/0000-0002-8251-4878
Jue D WangDepartment of Bacteriology, University of Wisconsin-Madison, Madison, WI, USA. wang@bact.wisc.edu.ORCID http://orcid.org/0000-0003-1503-170X
Gert BangeMax Planck Institute for Terrestrial Microbiology, Marburg, Germany. gert.bange@synmikro.uni-marburg.de.ORCID http://orcid.org/0000-0002-7826-0932

Funding

GRADUATE TRAINING IN MOLECULAR BIOSCIENCEST32GM007215 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HULL, CHRISTINA M · 1985 to 2018
$22.5M
The critical roles of (p)ppGpp in homeostasis and antibiotic tolerance in Gram positive bacteriaR35GM127088 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Jue D. Wang · 2018 to 2026
$3.9M
NIGMS NIH HHS R35 GM127088NIGMS NIH HHS T32 GM007215
6 · The paper itself

Abstract

Reversible lysine acetylation is a highly conserved post-translational modification across all domains of life controlling diverse cellular processes such as metabolism and gene expression. However, the regulation of protein acetylation remains poorly understood. Here, we report a regulatory system in Bacillus subtilis that controls the activity of the histone deacetylase (HDAC)-like protein AcuC, which has multiple substrates including acetyl-CoA synthetase and translation elongation factor. We show that AcuC is inhibited via formation of a stable complex with the hitherto uncharacterized protein AcuB. We furthermore demonstrate that the alarmone diadenosine tetraphosphate (Ap4A) binds to the cystathionine beta-synthase (CBS) domain of AcuB, thereby stabilizing AcuB and further enhancing the inhibition of AcuC. In summary, this study identifies AcuB as an Ap4A regulated deacetylation inhibitor, revealing a uncharacterized molecular mechanism to control HDAC-like proteins. Thus, the alarmone Ap4A modulates protein (de)acetylation, pointing towards a regulatory network that connects stress response, protein acetylation, and acetyl-CoA biosynthesis.

Indexed as

Bacillus subtilisBacterial ProteinsDinucleoside PhosphatesHistone DeacetylasesAcetylationCystathionine beta-SynthaseProtein BindingProtein Processing, Post-TranslationalBacterial ProteinsCystathionine beta-Synthasediadenosine tetraphosphateDinucleoside PhosphatesHistone Deacetylases

Identifiers

PMID41730913
PMCPMC13039410

What OpenQuestion holds

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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.