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Article

E2F-dependent histone acetylation and recruitment of the Tip60 acetyltransferase complex to chromatin in late G1.

Molecular and cellular biology - 1 May 2004

Taubert Stefan, Gorrini Chiara, Frank Scott R, Parisi Tiziana, Fuchs Miriam, Chan Ho-Man, Livingston David M, Amati Bruno

Abstract excerpt

E2F proteins can either activate or repress transcription. Following mitogenic stimulation, repressive E2F4-p130-histone deacetylase complexes dissociate from, while activating species (E2F1, -2, and -3) associate with, target promoters. Histones H3 and H4 simultaneously become hyperacetylated, but it remains unclear whether this is a prerequisite or a consequence of E2F binding. Here, we show that activating E2F...

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Identifiers

PMID: 15121871
DOI: 10.1128/MCB.24.10.4546-4556.2004
PMCID: PMC400446

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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