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Updated: May 22, 2026

Biochemical Assays for Analyzing Activities of ATP-dependent Chromatin Remodeling Enzymes
10:14

Biochemical Assays for Analyzing Activities of ATP-dependent Chromatin Remodeling Enzymes

Published on: October 25, 2014

Combinatorial histone modifications direct ATP-dependent chromatin remodeling by NURF to promoter-proximal

So Yeon Kwon1, Boyun Jang1, Valentina Grisan1

  • 1Department of Cancer and Genomic Sciences, School of Medical Sciences, College of Medicine and Health, University of Birmingham, Edgbaston B15 2TT, United Kingdom.

Nucleic Acids Research
|May 21, 2026
PubMed

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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.
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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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