Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin.

Full Abstract

Nucleosomes must be deacetylated behind elongating RNA polymerase II to prevent cryptic initiation of transcription within the coding region. RNA polymerase II signals for deacetylation through the methylation of histone H3 lysine 36 (H3K36), which provides the recruitment signal for the Rpd3S histone deacetylase complex (HDAC). The recognition of methyl H3K36 by Rpd3S requires the chromodomain of its Eaf3 subunit. Paradoxically, Eaf3 is also a subunit of the NuA4 acetyltransferase complex, yet NuA4 does not recognize methyl H3K36 nucleosomes. In Saccharomyces cerevisiae, we found that methyl H3K36 nucleosome recognition by Rpd3S also requires the plant homeobox domain (PHD) of its Rco1 subunit. Thus, the coupled chromo and PHD domains of Rpd3S specify recognition of the methyl H3K36 mark, demonstrating the first combinatorial domain requirement within a protein complex to read a specific histone code.

Author information

Author/s: Li, Bing (B); Gogol, Madelaine (M); Carey, Mike (M); Lee, Daeyoup (D); Seidel, Chris (C); Workman, Jerry L (JL);

Affiliation: Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA.

Journal and publication information

Publication Type: Journal Article; Research Support, N.I.H., Extramural

Journal: Science (New York, N.Y.) (Science), published in United States. (Language: eng)

Reference: 2007-May; vol 316 (issue 5827) : pp 1050-4

Dates: Created 2007/05/18; Completed 2007/06/06; Revised 2008/11/06;

PMID: 17510366, status: MEDLINE (last retrieved date: 2/18/2009)

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MeSH Headings (categories) shown below.

Acetylation
Acetyltransferases - chemistry; metabolism
Chromatin - metabolism
Chromatin Immunoprecipitation
DNA, Fungal - metabolism
Histone Acetyltransferases - chemistry; metabolism
Histone Code
Histone Deacetylases - chemistry; metabolism
Histones - metabolism
Methylation

Note: Bold headings indicate primary MeSH headings or qualifiers.

Associated Chemicals: Chromatin (0) ; DNA, Fungal (0) ; Histones (0) ; Nucleosomes (0) ; Protein Subunits (0) ; Saccharomyces cerevisiae Proteins (0) ; Yng2 protein, S cerevisiae (0) ; Acetyltransferases (EC 2.3.1.-) ; Eaf3 protein, S cerevisiae (EC 2.3.1.-) ; Histone Acetyltransferases (EC 2.3.1.48) ; NuA4 protein, S cerevisiae (EC 2.3.1.48) ; Histone Deacetylases (EC 3.5.1.-) ; RPD3 protein, S cerevisiae (EC 3.5.1.-)

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