PLoS Genetics · 2012 · 110 citations · 44 references
Life SciencesMolecular BiologyPlant BiologyEpigeneticsGene ExpressionTranscriptional RegulationPlant Epigenetic RegulationPlant Transcriptional RegulationPromoter RegulationTranscription In EukaryotesTranscriptional ControlTranscriptional Regulation In EukaryotesHistone H3 Lysine 4 MethylationPlant PromotersPlant Trithorax RegulationPoint MutationsTata-box Binding ProteinTranscription Elongation ControlTrithorax ActivationTrithorax Group Proteins
Tri-methylated H3 lysine 4 (H3K4me3) is associated with transcriptionally active genes, but its function in the transcription process is still unclear. Point mutations in the catalytic domain of ATX1 (ARABIDOPSIS TRITHORAX1), a H3K4 methyltransferase, and RNAi knockdowns of subunits of the AtCOMPASS-like (Arabidopsis Complex Proteins Associated with Set) were used to address this question. We demonstrate that both ATX1 and AtCOMPASS-like are required for high level accumulation of TBP (TATA-binding protein) and Pol II at promoters and that this requirement is independent of the catalytic histone modifying activity. However, the catalytic function is critically required for transcription as H3K4me3 levels determine the efficiency of transcription elongation. The roles of H3K4me3, ATX1, and AtCOMPASS-like may be of a general relevance for transcription of Trithorax-activated eukaryotic genes.
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Active genes are tri-methylated at K4 of histone H3
Helena Santos-Rosa, Robert Schneider, Andrew J. Bannister et al. · Nature · 2002 · 2.2K citations
Selective Anchoring of TFIID to Nucleosomes by Trimethylation of Histone H3 Lysine 4
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