Evidence map›Paper›PMID 19114561›Full record

ArticleMolecular and cellular biology2009

The H3K4 demethylase lid associates with and inhibits histone deacetylase Rpd3.

Nara Lee, Hediye Erdjument-Bromage, Paul Tempst, Richard S Jones, Yi Zhang

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
–field-weighted citation impact
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

48 citing papers in PubMed.

  1. Emerging role ofFrontiers in molecular neuroscience · 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

5 authors.

Nara LeeDepartment of Biochemistry and Biophysics, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7295. yi_zhang@med.unc.edu.
Hediye Erdjument-Bromage
Paul Tempst
Richard S Jones
Yi Zhang

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
Mechanisms of Polycomb SilencingR01GM068804 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZHANG, YI · 2003 to 2010
$2.1M
POLYCOMB-GROUP GENES AND GENE REGULATIONR01GM046567 · NIGMS · SOUTHERN METHODIST UNIVERSITY · PI JONES, RICHARD S · 1991 to 2006
$1.6M
Howard Hughes Medical InstituteNCI NIH HHS P30 CA008748NIGMS NIH HHS R01 GM046567NIGMS NIH HHS R01 GM068804
6 · The paper itself

Abstract

JmjC domain-containing proteins have been shown to possess histone demethylase activity. One of these proteins is the Drosophila histone H3 lysine 4 demethylase Little imaginal discs (Lid), which has been genetically classified as a Trithorax group protein. However, contrary to the supposed function of Lid in gene activation, the biochemical activity of this protein entails the removal of a histone mark that is correlated with active transcription. To understand the molecular mechanism behind the function of Lid, we have purified a Lid-containing protein complex from Drosophila embryo nuclear extracts. In addition to Lid, the complex contains Rpd3, CG3815/Drosophila Pf1, CG13367, and Mrg15. Rpd3 is a histone deacetylase, and along with Polycomb group proteins, which antagonize the function of Trithorax group proteins, it negatively regulates transcription. By reconstituting the Lid complex, we demonstrated that the demethylase activity of Lid is not affected by its association with other proteins. However, the deacetylase activity of Rpd3 is greatly diminished upon incorporation into the Lid complex. Thus, our finding that Lid antagonizes Rpd3 function provides an explanation for the genetic classification of Lid as a positive transcription regulator.

Indexed as

AnimalsCell ExtractsDrosophilaDrosophila ProteinsEmbryo, NonmammalianHistone Deacetylase 1Histone DeacetylasesHistone DemethylasesHistone-Lysine N-MethyltransferaseHistonesPolycomb-Group ProteinsProtein BindingRepressor ProteinsTranscription, GeneticCell ExtractsDrosophila ProteinsHDAC1 protein, DrosophilaHistone Deacetylase 1Histone DeacetylasesHistone DemethylasesHistone-Lysine N-MethyltransferaseHistonesLid protein, DrosophilaPolycomb-Group ProteinsRepressor Proteins

Identifiers

PMID19114561
PMCPMC2648242

What OpenQuestion holds

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Read underepoch 390

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.