ArticleProtein expression and purification2015
One-pot refolding of core histones from bacterial inclusion bodies allows rapid reconstitution of histone octamer.
Article in Protein expression and purification, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Coordinated neuron-specific splicing events restrict nucleosome engagement of the LSD1 histone demethylase complex.Cell reports · 2025Article
- Crucial roles of the BRCA1-BARD1 E3 ubiquitin ligase activity in homology-directed DNA repair.Molecular cell · 2023Article
- BRCA1/BARD1 intrinsically disordered regions facilitate chromatin recruitment and ubiquitylation.The EMBO journal · 2023Article
- Structural and mechanistic insights into the DNA glycosylase AAG-mediated base excision in nucleosome.Cell discovery · 2023Article
- Alternative Mechanisms for DNA Engagement by BET Bromodomain-Containing Proteins.Biochemistry · 2022Article
- Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin.Nature communications · 2021Article
- BRCA1/BARD1 site-specific ubiquitylation of nucleosomal H2A is directed by BARD1.Nature structural & molecular biology · 2021Article
- Cryoelectron Microscopy Structure of a Yeast Centromeric Nucleosome at 2.7 Å Resolution.Structure (London, England : 1993) · 2020Article
- Identification of DOT1L inhibitors by structure-based virtual screening adapted from a nucleoside-focused library.European journal of medicinal chemistry · 2020Article
- Cryo-EM structure of the human MLL1 core complex bound to the nucleosome.Nature communications · 2019Article
- Structural Basis of H2B Ubiquitination-Dependent H3K4 Methylation by COMPASS.Molecular cell · 2019Article
- Effects of histone H2B ubiquitylation on the nucleosome structure and dynamics.Nucleic acids research · 2018Article
- Article
- Preparative two-step purification of recombinant H1.0 linker histone and its domains.PloS one · 2017Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
We report an optimized method to purify and reconstitute histone octamer, which utilizes high expression of histones in inclusion bodies but eliminates the time consuming steps of individual histone purification. In the newly modified protocol, Xenopus laevis H2A, H2B, H3, and H4 are expressed individually into inclusion bodies of bacteria, which are subsequently mixed together and denatured in 8M guanidine hydrochloride. Histones are refolded and reconstituted into soluble octamer by dialysis against 2M NaCl, and metal-affinity purified through an N-terminal polyhistidine-tag added on the H2A. After cleavage of the polyhistidine-tag, histone octamer is further purified by size exclusion chromatography. We show that the nucleosomes reconstituted using the purified histone octamer above are fully functional. They serve as effective substrates for the histone methyltransferases DOT1L and MLL1. Small angle X-ray scattering further confirms that the reconstituted nucleosomes have correct structural integration of histone octamer and DNA as observed in the X-ray crystal structure. Our new protocol enables rapid reconstitution of histone octamer with an optimal yield. We expect this simplified approach to facilitate research using recombinant nucleosomes in vitro.
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