Evidence map›Paper›PMID 30540930›Full record

ArticleCell reports2018

SIRT7-Dependent Deacetylation of Fibrillarin Controls Histone H2A Methylation and rRNA Synthesis during the Cell Cycle.

Aishwarya Iyer-Bierhoff, Nicolai Krogh, Peter Tessarz, Thomas Ruppert, Henrik Nielsen, Ingrid Grummt

Open access · goldAbstract read
PubMed Publisher
In one paragraph

Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

57 citing papers in PubMed, 100 citations in OpenAlex.

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  13. SNORD80-guided 2'-O-methylation stabilizes the lncRNA GAS5 to regulate cellular stress responses.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. The dark side of SIRT7.Molecular and cellular biochemistry · 2024
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Aishwarya Iyer-BierhoffMolecular Biology of the Cell II, German Cancer Research Centre (DKFZ), DKFZ-Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH) Alliance, 69120 Heidelberg, Germany.
Nicolai KroghDepartment of Cellular and Molecular Medicine, University of Copenhagen, 2200N Copenhagen, Denmark.
Peter TessarzDepartment of Chromatin and Ageing, Max Planck Institute for Biology of Ageing, 50931 Cologne, Germany.
Thomas RuppertCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, 69120 Heidelberg, Germany.
Henrik NielsenDepartment of Cellular and Molecular Medicine, University of Copenhagen, 2200N Copenhagen, Denmark.
Ingrid GrummtMolecular Biology of the Cell II, German Cancer Research Centre (DKFZ), DKFZ-Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH) Alliance, 69120 Heidelberg, Germany. Electronic address: i.grummt@dkfz.de.
Heidelberg University · DEUniversity of Copenhagen · DKDKFZ-ZMBH Alliance · DEMax Planck Institute for Biology of Ageing · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fibrillarin (FBL) is a dual-function nucleolar protein that catalyzes 2'-O methylation of pre-rRNA and methylation of histone H2A at glutamine 104 (H2AQ104me). The mechanisms that regulate FBL activity are unexplored. Here, we show that FBL is acetylated at several lysine residues by the acetyltransferase CBP and deacetylated by SIRT7. While reversible acetylation does not impact FBL-mediated pre-rRNA methylation, hyperacetylation impairs the interaction of FBL with histone H2A and chromatin, thereby compromising H2AQ104 methylation (H2AQ104me) and rDNA transcription. SIRT7-dependent deacetylation of FBL ensures H2AQ104me and high levels of rRNA synthesis during interphase. At the onset of mitosis, nucleolar disassembly is accompanied by hyperacetylation of FBL, loss of H2AQ104me, and repression of polymerase I (Pol I) transcription. Overexpression of an acetylation-deficient, but not an acetylation-mimicking, FBL mutant restores H2AQ104me and transcriptional activity. The results reveal that SIRT7-dependent deacetylation impacts nucleolar activity by an FBL-driven circuitry that mediates cell-cycle-dependent fluctuation of rDNA transcription.

Indexed as

Cell CycleAcetylationCell LineChromosomal Proteins, Non-HistoneDNA, RibosomalGlutamineHistonesHumansMethylationMitosisProtein BindingRNA PrecursorsRNA Processing, Post-TranscriptionalRNA, RibosomalSirtuinsTranscription, GeneticChromosomal Proteins, Non-HistoneDNA, RibosomalfibrillarinGlutamineHistonesRNA PrecursorsRNA, RibosomalSIRT7 protein, humanSirtuinsacetylationcell cyclechromatinfibrillaringlutamine methylationhistone H2AnucleolusrRNASIRT7transcription

Identifiers

PMID30540930
OpenAlexW2905204058

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.