Evidence map›Paper›PMID 24100017›Full record

ArticleMolecular and cellular biology2013

Elements of the polycomb repressor SU(Z)12 needed for histone H3-K27 methylation, the interface with E(Z), and in vivo function.

Aswathy N Rai, Marcus L Vargas, Liangjun Wang, Erica F Andersen, Ellen L Miller, Jeffrey A Simon

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

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  7. iScience · 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

6 authors at 1 institution in 1 country.

Aswathy N RaiDepartment of Genetics, Cell Biology, and Development, University of Minnesota, and Graduate Program in Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA.
Marcus L Vargas
Liangjun Wang
Erica F Andersen
Ellen L Miller
Jeffrey A Simon
University of Minnesota · US

Funding

TRANSCRIPTIONAL REPRESSION BY POLYCOMB GROUP PRODUCTSR01GM049850 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI SIMON, JEFFREY A · 1996 to 2017
$4.8M
NIGMS NIH HHS GM49850NIGMS NIH HHS R01 GM049850
6 · The paper itself

Abstract

Polycomb repressive complex 2 (PRC2) is an essential chromatin-modifying enzyme that implements gene silencing. PRC2 methylates histone H3 on lysine-27 and is conserved from plants to flies to humans. In Drosophila melanogaster, PRC2 contains four core subunits: E(Z), SU(Z)12, ESC, and NURF55. E(Z) bears a SET domain that houses the enzyme active site. However, PRC2 activity depends upon critical inputs from SU(Z)12 and ESC. The stimulatory mechanisms are not understood. We present here functional dissection of the SU(Z)12 subunit. SU(Z)12 contains two highly conserved domains: an ∼140-amino-acid VEFS domain and a Cys2-His2 zinc finger (ZnF). Analysis of recombinant PRC2 bearing VEFS domain alterations, including some modeled after leukemia mutations, identifies distinct elements needed for SU(Z)12 assembly with E(Z) and stimulation of histone methyltransferase. The results define an extensive VEFS subdomain that organizes the SU(Z)12-E(Z) interface. Although the SU(Z)12 ZnF is not needed for methyltransferase in vitro, genetic rescue assays show that the ZnF is required in vivo. Chromatin immunoprecipitations reveal that this ZnF facilitates PRC2 binding to a genomic target. This study defines functionally critical SU(Z)12 elements, including key determinants of SU(Z)12-E(Z) communication. Together with recent findings, this illuminates PRC2 modulation by conserved inputs from its noncatalytic subunits.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsChromatinConserved SequenceDrosophila melanogasterDrosophila ProteinsHistone-Lysine N-MethyltransferaseHistonesMethylationMolecular Sequence DataNuclear ProteinsPolycomb Repressive Complex 2Protein Interaction Domains and MotifsProtein Interaction MappingProtein Processing, Post-TranslationalChromatinDrosophila ProteinsE(z) protein, DrosophilaHistone-Lysine N-MethyltransferaseHistonesNuclear ProteinsPolycomb Repressive Complex 2PRC2 protein, DrosophilaSu(z)12 protein, Drosophila

Identifiers

PMID24100017
PMCPMC3889545
OpenAlexW2157852477

What OpenQuestion holds

Textmetadata
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Registered trials

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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.