Evidence map›Paper›PMID 32895554›Full record

ArticleNature structural & molecular biology2020

Two HIRA-dependent pathways mediate H3.3 de novo deposition and recycling during transcription.

Júlia Torné, Dominique Ray-Gallet, Ekaterina Boyarchuk, Mickaël Garnier, Patricia Le Baccon, Antoine Coulon, Guillermo A Orsi, Geneviève Almouzni

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.9field-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

41 citing papers in PubMed, 74 citations in OpenAlex.

  1. Stress triggers global histone synthesis in the liver.bioRxiv : the preprint server for biology · 2026
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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

8 authors at 2 institutions in 2 countries.

Júlia TornéInstitut Curie, PSL Research University, CNRS UMR3664, Paris, France.
Dominique Ray-GalletInstitut Curie, PSL Research University, CNRS UMR3664, Paris, France.
Ekaterina BoyarchukInstitut Curie, PSL Research University, CNRS UMR3664, Paris, France.ORCID http://orcid.org/0000-0002-7691-6547
Mickaël GarnierInstitut Curie, PSL Research University, CNRS UMR3664, Paris, France.
Patricia Le BacconInstitut Curie, PSL Research University, CNRS UMR3664, Paris, France.
Antoine CoulonInstitut Curie, PSL Research University, CNRS UMR3664, Paris, France.ORCID http://orcid.org/0000-0003-4003-6043
Guillermo A OrsiInstitut Curie, PSL Research University, CNRS UMR3664, Paris, France. guillermo.orsi@inserm.fr.ORCID http://orcid.org/0000-0001-5139-1417
Geneviève AlmouzniInstitut Curie, PSL Research University, CNRS UMR3664, Paris, France. genevieve.almouzni@curie.fr.ORCID http://orcid.org/0000-0001-5570-0723
Centre National de la Recherche Scientifique · FRUniversité Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleosomes represent a challenge in regard to transcription. Histone eviction enables RNA polymerase II (RNAPII) progression through DNA, but compromises chromatin integrity. Here, we used the SNAP-tag system to distinguish new and old histones and monitor chromatin reassembly coupled to transcription in human cells. We uncovered a transcription-dependent loss of old histone variants H3.1 and H3.3. At transcriptionally active domains, H3.3 enrichment reflected both old H3.3 retention and new deposition. Mechanistically, we found that the histone regulator A (HIRA) chaperone is critical to processing both new and old H3.3 via different pathways. De novo H3.3 deposition is totally dependent on HIRA trimerization as well as on its partner ubinuclein 1 (UBN1), while antisilencing function 1 (ASF1) interaction with HIRA can be bypassed. By contrast, recycling of H3.3 requires HIRA but proceeds independently of UBN1 or HIRA trimerization and shows absolute dependency on ASF1-HIRA interaction. We propose a model whereby HIRA coordinates these distinct pathways during transcription to fine-tune chromatin states.

Indexed as

Signal TransductionTranscription, GeneticCell Cycle ProteinsHeLa CellsHistone ChaperonesHistonesHumansNuclear ProteinsProtein MultimerizationTranscription FactorsCell Cycle ProteinsHIRA protein, humanHistone ChaperonesHistonesNuclear ProteinsTranscription FactorsUBN1 protein, human

Identifiers

PMID32895554
OpenAlexW3083369579

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.