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Nucleosome Remodeling

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...

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A Method for H2A.Z/H2B Dimer Exchange Within Nucleosomes In Vitro.

Benoit Guillemette¹, Liette Laflamme¹, Luc Gaudreau²

¹Faculté des sciences, Département de biologie, Université de Sherbrooke, Sherbrooke, QC, Canada.

Methods in Molecular Biology (Clifton, N.J.)

|April 21, 2025

Summary

This study presents a new assay to measure histone exchange activity, crucial for gene regulation. The assay uses recombinant human p400 and Flag-tagged H2A.Z/H2B dimers to detect histone variant exchange in vitro.

Keywords:

Chromatin H2A.Z Histone variant Htz1 Nucleosome SRCAP Swr1 Tip60 p400

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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

Area of Science:

Epigenetics and Chromatin Biology
Molecular Biology
Biochemistry

Background:

Histone variant H2A.Z plays a key role in gene expression and genomic stability.
H2A.Z incorporation into nucleosomes involves the exchange of H2A-H2B dimers with H2A.Z-H2B dimers.
Chromatin remodeling complexes, like the yeast Swr1 complex, facilitate this histone exchange.

Purpose of the Study:

To develop and describe an in vitro assay for measuring histone exchange activity.
To utilize recombinant human p400 and Flag-tagged H2A.Z/H2B dimers for this assay.
To provide a method adaptable for studying other histone exchange complexes.

Main Methods:

Recombinant human p400 expressed in insect Sf9 cells was used.
The assay employed immobilized mononucleosomes.
Flag-tagged H2A.Z/H2B dimers were used for histone exchange.
Histone exchange was quantified using Western blot analysis.

Main Results:

Successfully established an in vitro assay to measure histone exchange activity.
Demonstrated the utility of the assay with recombinant human p400.
The assay provides a quantifiable measure of histone variant exchange.

Conclusions:

The developed assay is effective for measuring histone exchange activity in vitro.
This method allows for the characterization of histone exchange complexes, including human p400.
The assay is versatile and can be adapted for various species and histone exchange factors.