ArticleFrontiers in cell and developmental biology2020
The Use of Mononucleosome Immunoprecipitation for Analysis of Combinatorial Histone Post-translational Modifications and Purification of Nucleosome-Interacting Proteins.
Article in Frontiers in cell and developmental biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Chemical biology tools for studying histone post-translational modifications.Cell chemical biology · 2026Review
- H4K16 acylations destabilize chromatin architecture and facilitate transcriptional response during metabolic perturbations.Molecular cell · 2026Article
- H2BK120ub and its reader RNF169 sequentially regulate replication fork remodeling and stability.The EMBO journal · 2025Article
- PBAF/cBAF reorganization on H3.3 chromatin regulates BMAL1 activity in the absence of circadian negative feedback.Nature communications · 2025Article
- Mechanistic insights into DNA binding by BD1 of the TAF1 tandem bromodomain module.The Biochemical journal · 2025Article
- Chicken Erythrocyte: Epigenomic Regulation of Gene Activity.International journal of molecular sciences · 2023Review
- SHP-1 dephosphorylates histone H2B to facilitate its ubiquitination during transcription.The EMBO journal · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
The nucleosome is the principal structural unit of chromatin. Although many studies focus on individual histone post-translational modifications (PTMs) in isolation, it is important to recognize that multiple histone PTMs can function together or cross-regulate one another within the nucleosome context. In addition, different modifications or histone-binding surfaces can synergize to stabilize the binding of nuclear factors to nucleosomes. To facilitate these types of studies, we present here a step-by-step protocol for isolating high yields of mononucleosomes for biochemical analyses. Furthermore, we discuss differences and variations of the basic protocol used in different publications and characterize the relative abundance of selected histone PTMs and chromatin-binding proteins in the different chromatin fractions obtained by this method.
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