Evidence map›Paper›PMID 33445503›Full record

ArticleInternational journal of molecular sciences2021

JAZF1, A Novel p400/TIP60/NuA4 Complex Member, Regulates H2A.Z Acetylation at Regulatory Regions.

Tara Procida, Tobias Friedrich, Antonia P M Jack, Martina Peritore, Clemens Bönisch, H Christian Eberl, Nadine Daus, Konstantin Kletenkov, Andrea Nist, Thorsten Stiewe and 4 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

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  16. Variants inFrontiers in genetics · 2023
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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

14 authors at 4 institutions in 1 country.

Tara ProcidaInstitute for Genetics, Justus-Liebig University Giessen, 35392 Giessen, Germany.
Tobias FriedrichInstitute for Genetics, Justus-Liebig University Giessen, 35392 Giessen, Germany.
Antonia P M JackDepartment of Molecular Biology, BioMedical Center (BMC), Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany.
Martina PeritoreDepartment of Molecular Biology, BioMedical Center (BMC), Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany.ORCID 0000-0003-2250-4528
Clemens BönischDepartment of Molecular Biology, BioMedical Center (BMC), Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany.
H Christian EberlDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.ORCID 0000-0002-4159-5958
Nadine DausInstitute for Genetics, Justus-Liebig University Giessen, 35392 Giessen, Germany.
Konstantin KletenkovInstitute for Genetics, Justus-Liebig University Giessen, 35392 Giessen, Germany.
Andrea NistGenomics Core Facility, Institute of Molecular Oncology, Member of the German Center for Lung Research (DZL), Philipps-University Marburg, 35043 Marburg, Germany.
Thorsten StieweGenomics Core Facility, Institute of Molecular Oncology, Member of the German Center for Lung Research (DZL), Philipps-University Marburg, 35043 Marburg, Germany.ORCID 0000-0003-0134-7826
Tilman BorggrefeInstitute for Biochemistry, Justus-Liebig-University Giessen, 35392 Giessen, Germany.
Matthias MannDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Marek BartkuhnInstitute for Genetics, Justus-Liebig University Giessen, 35392 Giessen, Germany.
Sandra B HakeInstitute for Genetics, Justus-Liebig University Giessen, 35392 Giessen, Germany.
Justus-Liebig-Universität Gießen · DELudwig-Maximilians-Universität München · DEGerman Center for Lung Research · DEMax Planck Institute of Biochemistry · DE

Funding

DFG HA 5437/6-1
6 · The paper itself

Abstract

Histone variants differ in amino acid sequence, expression timing and genomic localization sites from canonical histones and convey unique functions to eukaryotic cells. Their tightly controlled spatial and temporal deposition into specific chromatin regions is accomplished by dedicated chaperone and/or remodeling complexes. While quantitatively identifying the chaperone complexes of many human H2A variants by using mass spectrometry, we also found additional members of the known H2A.Z chaperone complexes p400/TIP60/NuA4 and SRCAP. We discovered JAZF1, a nuclear/nucleolar protein, as a member of a p400 sub-complex containing MBTD1 but excluding ANP32E. Depletion of JAZF1 results in transcriptome changes that affect, among other pathways, ribosome biogenesis. To identify the underlying molecular mechanism contributing to JAZF1's function in gene regulation, we performed genome-wide ChIP-seq analyses. Interestingly, depletion of JAZF1 leads to reduced H2A.Z acetylation levels at > 1000 regulatory sites without affecting H2A.Z nucleosome positioning. Since JAZF1 associates with the histone acetyltransferase TIP60, whose depletion causes a correlated H2A.Z deacetylation of several JAZF1-targeted enhancer regions, we speculate that JAZF1 acts as chromatin modulator by recruiting TIP60's enzymatic activity. Altogether, this study uncovers JAZF1 as a member of a TIP60-containing p400 chaperone complex orchestrating H2A.Z acetylation at regulatory regions controlling the expression of genes, many of which are involved in ribosome biogenesis.

Indexed as

Regulatory Sequences, Nucleic AcidAcetylationCell LineChromatin Assembly and DisassemblyComputational BiologyCo-Repressor ProteinsDNA-Binding ProteinsDNA HelicasesEnhancer Elements, GeneticGene Expression RegulationGenomicsHistonesHumansIntronsLysine Acetyltransferase 5Molecular ChaperonesCo-Repressor ProteinsDNA-Binding ProteinsDNA HelicasesEP400 protein, humanHistonesJAZF1 protein, humanKAT5 protein, humanLysine Acetyltransferase 5Molecular ChaperonesMultiprotein ComplexesTranscription Factorsacetylationenhancergene regulationH2A.Zhistone variantsJAZF1ribosomeTIP60

Identifiers

PMID33445503
PMCPMC7826843
OpenAlexW3120159706

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.