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Related Concept Videos

Nucleosome Remodeling02:54

Nucleosome Remodeling

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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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Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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Histone Modification02:32

Histone Modification

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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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Spreading of Chromatin Modifications02:25

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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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The writer...
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The Nucleosome Core Particle01:12

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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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Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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The Nucleosome01:19

The Nucleosome

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Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
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Updated: Sep 28, 2025

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
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Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

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Acidic patch histone mutations and their effects on nucleosome remodeling.

Hai T Dao1, Linh T D Pham2

  • 1Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, U.S.A.

Biochemical Society Transactions
|March 31, 2022
PubMed
Summary

Cancer-associated mutations in the nucleosome acidic patch alter how chromatin remodelers function. These histone mutations lead to unexpected changes in chromatin structure, impacting gene regulation.

Keywords:
acidic patchasymmetric nucleosomehistone mutationnucleosome remodeling

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cancer Biology

Background:

  • The nucleosome acidic patch is a key regulatory site on histones.
  • It interacts with nuclear proteins, including ATP-dependent chromatin remodelers (SWI/SNF, ISWI, CHD, INO80).
  • Cancer mutations frequently occur in histone genes, including those affecting the acidic patch.

Purpose of the Study:

  • To review how cancer-related acidic patch histone mutations affect nucleosome remodeling.
  • To summarize findings on remodeler interactions with wild-type and mutant acidic patches.
  • To discuss models for chromatin changes due to acidic patch mutations.

Main Methods:

  • In vitro chromatin reconstitution to create physiologically relevant nucleosomes.
  • Biochemical investigation of nucleosome remodeling outcomes using wild-type and mutant histones.
  • Analysis of genome-wide sequencing data from human cancers.

Main Results:

  • Different remodeler families exhibit distinct interactions with wild-type versus mutant acidic patches.
  • Acidic patch mutations lead to unexpected nucleosome remodeling outcomes.
  • These alterations have significant implications for chromatin structure and function.

Conclusions:

  • Cancer mutations in the nucleosome acidic patch can reprogram remodeler activity.
  • This reprogramming can lead to altered chromatin landscapes with potential roles in cancer.
  • Understanding these interactions is crucial for deciphering cancer-related chromatin alterations.