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Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4.

Cell | Oct 5, 2007

http://www.ncbi.nlm.nih.gov/pubmed/17884155

Trimethylation of histone H3 at lysine 4 (H3K4me3) is regarded as a hallmark of active human promoters, but it remains unclear how this posttranslational modification links to transcriptional activation. Using a stable isotope labeling by amino acids in cell culture (SILAC)-based proteomic screening we show that the basal transcription factor TFIID directly binds to the H3K4me3 mark via the plant homeodomain (PHD) finger of TAF3. Selective loss of H3K4me3 reduces transcription from and TFIID binding to a subset of promoters in vivo. Equilibrium binding assays and competition experiments show that the TAF3 PHD finger is highly selective for H3K4me3. In transient assays, TAF3 can act as a transcriptional coactivator in a PHD finger-dependent manner. Interestingly, asymmetric dimethylation of H3R2 selectively inhibits TFIID binding to H3K4me3, whereas acetylation of H3K9 and H3K14 potentiates TFIID interaction. Our experiments reveal crosstalk between histone modifications and the transcription factor TFIID. This has important implications for regulation of RNA polymerase II-mediated transcription in higher eukaryotes.

Pubmed ID: 17884155 RIS Download

Mesh terms: Acetylation | Amino Acid Sequence | Animals | Gene Expression Regulation | HeLa Cells | Histones | Homeodomain Proteins | Humans | Lysine | Macromolecular Substances | Methylation | Mice | Molecular Sequence Data | Nucleosomes | RNA, Messenger | Recombinant Fusion Proteins | Transcription Factor TFIID | Tumor Suppressor Proteins | Zinc Fingers

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