RSC Exploits Histone Acetylation to Abrogate the Nucleosomal Block to RNA Polymerase II Elongation

Michael Carey, Bing Li, Jerry L. Workman

Research output: Contribution to journalArticle

132 Citations (Scopus)

Abstract

The coordinated action of histone acetyltransferases (HATs) and ATP-dependent chromatin remodeling enzymes in promoter-dependent transcription initiation represents a paradigm for how epigenetic information regulates gene expression. However, little is known about how such enzymes function during transcription elongation. Here, we investigated the role of RSC, a bromodomain-containing ATPase, in nucleosome transcription in vitro. Purified S. cerevisiae RNA polymerase II (Pol II) arrests at two primary locations on a positioned mononucleosome. RSC stimulates passage of Pol II through these sites. The function of RSC in elongation requires the energy of ATP hydrolysis. Moreover, the SAGA and NuA4 HATs strongly stimulated RSC's effect on elongation. The stimulation correlates closely with acetyl-CoA-dependent recruitment of RSC to nucleosomes. Thus, RSC can recognize acetylated nucleosomes and facilitate passage of Pol II through them. These data support the view that histone modifications regulate accessibility of the coding region to Pol II.

Original languageEnglish (US)
Pages (from-to)481-487
Number of pages7
JournalMolecular Cell
Volume24
Issue number3
DOIs
StatePublished - Nov 3 2006

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Nucleosomes
RNA Polymerase II
Acetylation
Histones
Histone Acetyltransferases
Histone Code
Adenosine Triphosphate
Acetyl Coenzyme A
Chromatin Assembly and Disassembly
Enzymes
Epigenomics
Saccharomyces cerevisiae
Adenosine Triphosphatases
Hydrolysis
Gene Expression

Keywords

  • DNA

ASJC Scopus subject areas

  • Molecular Biology

Cite this

RSC Exploits Histone Acetylation to Abrogate the Nucleosomal Block to RNA Polymerase II Elongation. / Carey, Michael; Li, Bing; Workman, Jerry L.

In: Molecular Cell, Vol. 24, No. 3, 03.11.2006, p. 481-487.

Research output: Contribution to journalArticle

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