Evidence map›Paper›PMID 12588981›Full record

ArticleMolecular and cellular biology2003

Balance between acetylation and methylation of histone H3 lysine 9 on the E2F-responsive dihydrofolate reductase promoter.

Estelle Nicolas, Christine Roumillac, Didier Trouche

Abstract read
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Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

43 citing papers in PubMed.

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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

3 authors.

Estelle NicolasLaboratoire de Biologie Moléculaire Eucaryote, UMR 5099 CNRS, IFR 109, Toulouse, France.
Christine Roumillac
Didier Trouche

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epigenetic marks that specify silent heterochromatic domains in eucaryotic genomes include methylation of histone H3 lysine 9. Strikingly, active loci in the vicinity of silent domains are sometimes characterized by acetylation of histone H3 lysine 9, suggesting that the balance between these two competitive modifications is important for the establishment of specific chromatin structures. Some euchromatic genes, targeted by the retinoblastoma protein Rb, are also believed to be regulated by histone H3 lysine 9 methylation. Here, we study the dihydrofolate reductase promoter, which is repressed in G0 and at the beginning of G1 by p107 or p130, two Rb-related proteins. We found that these two pocket proteins share with Rb the ability to associate with the histone methyl transferase SUV39H1. SUV39H1 can be recruited to the E2F transcription factor and functions as a transcriptional corepressor. With ChIP assays followed by real-time PCR, we showed that K9 of histone H3 evolves from a hypermethylated state in G0 to a hyperacetylated state at the G1/S transition. Taken together, these results indicate that the temporal regulation of euchromatic promoters may involve controlling the balance between methylation and acetylation of histone H3 lysine 9, a feature previously described for the spatial regulation of chromatin function.

Indexed as

Cell Cycle ProteinsDNA-Binding ProteinsProteins3T3 CellsAnimalsBlood ProteinsBlotting, WesternCell CycleCell LineChromatinE2F Transcription FactorsG1 PhaseGlutathione TransferaseHistonesHumansLysineBlood ProteinsCell Cycle ProteinsChromatinDNA-Binding ProteinsE2F Transcription FactorsGlutathione TransferaseHistonesLysineNuclear ProteinsProtein IsoformsProteinsRBL1 protein, humanRbl1 protein, mouseRBL2 protein, humanRbl2 protein, mouseRecombinant Fusion ProteinsRetinoblastoma-Like Protein p107Retinoblastoma-Like Protein p130Tetrahydrofolate DehydrogenaseTranscription Factors

Identifiers

PMID12588981
PMCPMC151719

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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.