Purification of Recombinant Histones and Mononucleosome Assembly

The nucleosome is the basic unit of chromatin. Each nucleosome is composed of a little less than two turns of DNA wrapped around a set of eight proteins called histones, which are known as a histone octamer. Each histone octamer is composed of two copies each of the histone proteins H2A, H2B, H3, and H4. Nucleosomes play an important role in gene expression and regulation. While previous protocols use HPLC (high-performance liquid chromatography) to purify each histone and, after octamer reconstitution, subsequent FPLC (fast protein liquid chromatography) to purify the octamers. Here we present a method to carry out octamer reconstitution and mononucleosome assembly with FPLC only. This basic protocol describes a procedure for histone purification from Escherichia coli (E. coli), their subsequent reconstitution as octamers, and assembly into mononucleosomes in vitro. Through this protocol, histone octamers and mononucleosomes can be reconstituted on a large scale without the use of HPLC. Overall, this protocol describes an effective new method for the reconstitution of octamers and assembly of mononucleosomes. © 2025 Wiley Periodicals LLC. Basic Protocol: Purification of recombinant histones and mononucleosome assembly.

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Publication Details

Journal
Current Protocols
Published
2025-05-01
DOI
https://doi.org/10.1002/cpz1.70155
Citations
2
Primary Topic
Genomics and Chromatin Dynamics
Type
article
Field-Weighted Citation Impact
1.61
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article

Purification of Recombinant Histones and Mononucleosome Assembly

Jingjun Hong, Yiming Zhao
2 citations
Current Protocols
Genomics and Chromatin Dynamics
1.61
article

Purification of Recombinant Histones and Mononucleosome Assembly

Jingjun Hong, Yiming Zhao
article en
2 citations

Abstract

The nucleosome is the basic unit of chromatin. Each nucleosome is composed of a little less than two turns of DNA wrapped around a set of eight proteins called histones, which are known as a histone octamer. Each histone octamer is composed of two copies each of the histone proteins H2A, H2B, H3, and H4. Nucleosomes play an important role in gene expression and regulation. While previous protocols use HPLC (high-performance liquid chromatography) to purify each histone and, after octamer reconstitution, subsequent FPLC (fast protein liquid chromatography) to purify the octamers. Here we present a method to carry out octamer reconstitution and mononucleosome assembly with FPLC only. This basic protocol describes a procedure for histone purification from Escherichia coli (E. coli), their subsequent reconstitution as octamers, and assembly into mononucleosomes in vitro. Through this protocol, histone octamers and mononucleosomes can be reconstituted on a large scale without the use of HPLC. Overall, this protocol describes an effective new method for the reconstitution of octamers and assembly of mononucleosomes. © 2025 Wiley Periodicals LLC. Basic Protocol: Purification of recombinant histones and mononucleosome assembly.

Current ProtocolsVol. 5(5)
Anhui University (CN), Hefei Institutes of Physical Science (CN)
Openalex Percentile: Top 17%
Genomics and Chromatin Dynamics
1.61
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Purification of Recombinant Histones and Mononucleosome Assembly — Jingjun Hong, Yiming Zhao · Current Protocols (2025) | TGRS Research Map | TGRS