Evidence map›Paper›PMID 24843044›Full record

ArticleThe EMBO journal2014

Eaf5/7/3 form a functionally independent NuA4 submodule linked to RNA polymerase II-coupled nucleosome recycling.

Dorine Rossetto, Myriam Cramet, Alice Y Wang, Anne-Lise Steunou, Nicolas Lacoste, Julia M Schulze, Valérie Côté, Julie Monnet-Saksouk, Sandra Piquet, Amine Nourani and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2014. 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
2.6field-weighted citation impact, top 10% 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, 64 citations in OpenAlex.

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  11. Structure of the NuA4 histone acetyltransferase complex.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

12 authors at 3 institutions in 1 country.

Dorine RossettoSt-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center Centre de Recherche du CHU de Québec-Axe Oncologie Hôtel-Dieu de Québec, Quebec City, QC, Canada.
Myriam CrametSt-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center Centre de Recherche du CHU de Québec-Axe Oncologie Hôtel-Dieu de Québec, Quebec City, QC, Canada.
Alice Y WangCenter for Molecular Medicine and Therapeutics, Child and Family Research Institute, Vancouver, BC, Canada.
Anne-Lise SteunouSt-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center Centre de Recherche du CHU de Québec-Axe Oncologie Hôtel-Dieu de Québec, Quebec City, QC, Canada.
Nicolas LacosteSt-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center Centre de Recherche du CHU de Québec-Axe Oncologie Hôtel-Dieu de Québec, Quebec City, QC, Canada.
Julia M SchulzeCenter for Molecular Medicine and Therapeutics, Child and Family Research Institute, Vancouver, BC, Canada.
Valérie CôtéSt-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center Centre de Recherche du CHU de Québec-Axe Oncologie Hôtel-Dieu de Québec, Quebec City, QC, Canada.
Julie Monnet-SaksoukSt-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center Centre de Recherche du CHU de Québec-Axe Oncologie Hôtel-Dieu de Québec, Quebec City, QC, Canada.
Sandra PiquetSt-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center Centre de Recherche du CHU de Québec-Axe Oncologie Hôtel-Dieu de Québec, Quebec City, QC, Canada.
Amine NouraniSt-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center Centre de Recherche du CHU de Québec-Axe Oncologie Hôtel-Dieu de Québec, Quebec City, QC, Canada.
Michael S KoborCenter for Molecular Medicine and Therapeutics, Child and Family Research Institute, Vancouver, BC, Canada.
Jacques CôtéSt-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center Centre de Recherche du CHU de Québec-Axe Oncologie Hôtel-Dieu de Québec, Quebec City, QC, Canada Jacques.Cote@crhdq.ulaval.ca.
Hôtel-Dieu de Québec · CAUniversité Laval · CAChild and Family Research Institute · CA

Funding

Canadian Institutes of Health Research MOP-119383Canadian Institutes of Health Research MOP-14308Canadian Institutes of Health Research MOP-81245
6 · The paper itself

Abstract

The NuA4 histone acetyltransferase complex is required for gene regulation, cell cycle progression, and DNA repair. Dissection of the 13-subunit complex reveals that the Eaf7 subunit bridges Eaf5 with Eaf3, a H3K36me3-binding chromodomain protein, and this Eaf5/7/3 trimer is anchored to NuA4 through Eaf5. This trimeric subcomplex represents a functional module, and a large portion exists in a native form outside the NuA4 complex. Gene-specific and genome-wide location analyses indicate that Eaf5/7/3 correlates with transcription activity and is enriched over the coding region. In agreement with a role in transcription elongation, the Eaf5/7/3 trimer interacts with phosphorylated RNA polymerase II and helps its progression. Loss of Eaf5/7/3 partially suppresses intragenic cryptic transcription arising in set2 mutants, supporting a role in nucleosome destabilization. On the other hand, loss of the trimer leads to an increase of replication-independent histone exchange over the coding region of transcribed genes. Taken together, these results lead to a model where Eaf5/7/3 associates with elongating polymerase to promote the disruption of nucleosomes in its path, but also their refolding in its wake.

Indexed as

Models, BiologicalAcetyltransferasesBlotting, WesternChromatin ImmunoprecipitationGene Expression Regulation, FungalHistone AcetyltransferasesMultiprotein ComplexesNucleosomesReverse Transcriptase Polymerase Chain ReactionRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAcetyltransferasesEaf3 protein, S cerevisiaeEaf5 protein, S cerevisiaeEaf7 protein, S cerevisiaeHistone AcetyltransferasesMultiprotein ComplexesNuA4 protein, S cerevisiaeNucleosomesRNA Polymerase IISaccharomyces cerevisiae Proteinshistone acetylationNuA4nucleosome dynamicstranscription elongation

Identifiers

PMID24843044
PMCPMC4194127
OpenAlexW1967074686

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.