ArticleProtein science : a publication of the Protein Society2022
Time Resolved-Fluorescence Resonance Energy Transfer platform for quantitative nucleosome binding and footprinting.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- BRD4 binds the nucleosome via both histone and DNA interactions.Molecular cell · 2026Article
- Different modes of engagement with the nucleosome acidic patch yield distinct functional outcomes.Nucleic acids research · 2026Article
- Different modes of engagement with the nucleosome acidic patch yield distinct functional outcomes.bioRxiv : the preprint server for biology · 2026Article
- Post-translational modification of H2B C-terminal helix regulates nucleosome interactions and chromatin signaling.Nucleic acids research · 2025Article
- One Tracer, Dual Platforms: Unlocking Versatility of Fluorescent Probes in TR-FRET and NanoBRET Target Engagement Assays.ACS medicinal chemistry letters · 2025Article
- PELP1 coordinates the modular assembly and enzymatic activity of the rixosome complex.Science advances · 2025Article
- Potent and selective SETDB1 covalent negative allosteric modulator reduces methyltransferase activity in cells.Nature communications · 2025Article
- Development of Biochemical and Cellular Probes to Study RIPK1 Target Engagement.ACS medicinal chemistry letters · 2024Article
- Dual engagement of the nucleosomal acidic patches is essential for deposition of histone H2A.Z by SWR1C.eLife · 2024Article
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- Structural basis of paralog-specific KDM2A/B nucleosome recognition.Nature chemical biology · 2023Article
- Cryo-EM structure of the human Sirtuin 6-nucleosome complex.Science advances · 2023Article
- Targeted Approaches to HER2-Low Breast Cancer: Current Practice and Future Directions.Cancers · 2022Review
- Time Resolved-Fluorescence Resonance Energy Transfer platform for quantitative nucleosome binding and footprinting.Protein science : a publication of the Protein Society · 2022Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Quantitative analysis of chromatin protein-nucleosome interactions is essential to understand regulation of genome-templated processes. However, current methods to measure nucleosome interactions are limited by low throughput, low signal-to-noise, and/or the requirement for specialized instrumentation. Here, we report a Lanthanide Chelate Excite Time-Resolved Fluorescence Resonance Energy Transfer (LANCE TR-FRET) assay to efficiently quantify chromatin protein-nucleosome interactions. The system makes use of commercially available reagents, offers robust signal-to-noise with minimal sample requirements, uses a conventional fluorescence microplate reader, and can be adapted for high-throughput workflows. We determined the nucleosome-binding affinities of several chromatin proteins and complexes, which are consistent with measurements obtained through orthogonal biophysical methods. We also developed a TR-FRET competition assay for high-resolution footprinting of chromatin protein-nucleosome interactions. Finally, we set up a TR-FRET competition assay using the LANA peptide to quantitate nucleosome acidic patch binding. We applied this assay to establish a proof-of-principle for regulation of nucleosome acidic patch binding by methylation of chromatin protein arginine anchors. Overall, our TR-FRET assays allow facile, high-throughput quantification of chromatin interactions and are poised to complement mechanistic chromatin biochemistry, structural biology, and drug discovery programs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.