Related Experiment Video
Updated: Jul 3, 2026

Profiling of H3K4me3 Modification in Plants using Cleavage under Targets and Tagmentation
Published on: April 22, 2022
Structural insight into the recognition of the H3K4me3 mark by the TFIID subunit TAF3
Hugo van Ingen1, Frederik M A van Schaik, Hans Wienk
1Bijvoet Centre for Biomolecular Research, Utrecht University, 3584 CH Utrecht, The Netherlands.
Abstract:
Trimethylation of lysine residue K4 of histone H3 (H3K4me3) strongly correlates with active promoters for RNA polymerase II-transcribed genes. Several reader proteins, including the basal transcription factor TFIID, for this nucleosomal mark have been identified. Its TAF3 subunit specifically binds the H3K4me3 mark via its conserved plant homeodomain (PHD) finger. Here, we report the solution structure of the TAF3-PHD finger and its complex with an H3K4me3 peptide. Using a combination of NMR, mutagenesis, and affinity measurements, we reveal the structural basis of binding affinity, methylation-state specificity, and crosstalk with asymmetric dimethylation of R2. A unique local structure rearrangement in the K4me3-binding pocket of TAF3 due to a conserved sequence insertion underscores the requirement for cation-pi interactions by two aromatic residues. Interference by asymmetric dimethylation of arginine 2 suggests that a H3R2/K4 "methyl-methyl" switch in the histone code dynamically regulates TFIID-promoter association.
More Related Videos
Related Concept Videos
General Transcription Factors
Histone Modification
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Transcription Elongation Factors
The transcription elongation is regulated via pausing of RNA polymerase on several occasions during transcription. In bacteria, these halts are necessary because the transcription of DNA into mRNA is coupled to the translation of that mRNA into a...
Total Internal Reflection Fluorescence Microscopy

