Evidence map›Paper›PMID 31036553›Full record

ArticleThe EMBO journal2019

The Nucleosome Remodelling and Deacetylation complex suppresses transcriptional noise during lineage commitment.

Thomas Burgold, Michael Barber, Susan Kloet, Julie Cramard, Sarah Gharbi, Robin Floyd, Masaki Kinoshita, Meryem Ralser, Michiel Vermeulen, Nicola Reynolds and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

35 citing papers in PubMed, 65 citations in OpenAlex.

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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 2 institutions in 2 countries.

Thomas BurgoldWellcome- MRC Stem Cell Institute, University of Cambridge, Cambridge, UK.
Michael BarberWellcome- MRC Stem Cell Institute, University of Cambridge, Cambridge, UK.
Susan KloetDepartment of Molecular Biology, Faculty of Science, Radboud Institute for Molecular Life Sciences, Oncode Institute, Radboud University, Nijmegen, The Netherlands.
Julie CramardWellcome- MRC Stem Cell Institute, University of Cambridge, Cambridge, UK.
Sarah GharbiWellcome- MRC Stem Cell Institute, University of Cambridge, Cambridge, UK.
Robin FloydWellcome- MRC Stem Cell Institute, University of Cambridge, Cambridge, UK.
Masaki KinoshitaWellcome- MRC Stem Cell Institute, University of Cambridge, Cambridge, UK.
Meryem RalserWellcome- MRC Stem Cell Institute, University of Cambridge, Cambridge, UK.
Michiel VermeulenDepartment of Molecular Biology, Faculty of Science, Radboud Institute for Molecular Life Sciences, Oncode Institute, Radboud University, Nijmegen, The Netherlands.ORCID 0000-0003-0836-6894
Nicola ReynoldsWellcome- MRC Stem Cell Institute, University of Cambridge, Cambridge, UK.
Sabine DietmannWellcome- MRC Stem Cell Institute, University of Cambridge, Cambridge, UK.
Brian HendrichWellcome- MRC Stem Cell Institute, University of Cambridge, Cambridge, UK brian.hendrich@cscr.cam.ac.uk.ORCID 0000-0002-0231-3073
Wellcome/MRC Cambridge Stem Cell Institute · GBRadboud University Nijmegen · NL

Funding

Medical Research Council MC_PC_12009Wellcome Trust
6 · The paper itself

Abstract

Multiprotein chromatin remodelling complexes show remarkable conservation of function amongst metazoans, even though components present in invertebrates are often found as multiple paralogous proteins in vertebrate complexes. In some cases, these paralogues specify distinct biochemical and/or functional activities in vertebrate cells. Here, we set out to define the biochemical and functional diversity encoded by one such group of proteins within the mammalian Nucleosome Remodelling and Deacetylation (NuRD) complex: Mta1, Mta2 and Mta3. We find that, in contrast to what has been described in somatic cells, MTA proteins are not mutually exclusive within embryonic stem (ES) cell NuRD and, despite subtle differences in chromatin binding and biochemical interactions, serve largely redundant functions. ES cells lacking all three MTA proteins exhibit complete NuRD loss of function and are viable, allowing us to identify a previously unreported function for NuRD in reducing transcriptional noise, which is essential for maintaining a proper differentiation trajectory during early stages of lineage commitment.

Indexed as

Transcription, GeneticAnimalsCell DifferentiationCell LineageCells, CulturedCellular ReprogrammingDNA-Binding ProteinsEmbryo, MammalianGene Expression Regulation, DevelopmentalMi-2 Nucleosome Remodeling and Deacetylase ComplexMiceMice, KnockoutMouse Embryonic Stem CellsNeoplasm ProteinsRepressor ProteinsSignal-To-Noise RatioDNA-Binding ProteinsMbd3 protein, mouseMi-2 Nucleosome Remodeling and Deacetylase ComplexMta1 protein, mouseMta2 protein, mouseMta3 protein, mouseNeoplasm ProteinsRepressor ProteinsTrans-ActivatorsTranscription FactorschromatinES Celllineage commitmentNuRDtranscription

Identifiers

PMID31036553
PMCPMC6576150
OpenAlexW2943151778

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.