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Related Concept Videos

Histone Modification02:32

Histone Modification

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.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Histone Modification02:32

Histone Modification

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.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
The Nucleosome01:19

The Nucleosome

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.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...
The Nucleosome02:33

The Nucleosome

DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to 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.
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...

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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
06:32

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Published on: March 9, 2022

A combinatorial H4 tail library for exploring the histone code.

Adam L Garske1, Gheorghe Craciun, John M Denu

  • 1Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706-1532, USA.

Biochemistry
|July 12, 2008
PubMed
Summary
This summary is machine-generated.

Researchers created a histone H4 modification library to study proteins that read the histone code. They found that K20 methylation is key for binding, while other modifications can alter this interaction.

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Generation of Native Chromatin Immunoprecipitation Sequencing Libraries for Nucleosome Density Analysis
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Generation of Native Chromatin Immunoprecipitation Sequencing Libraries for Nucleosome Density Analysis

Published on: December 12, 2017

Area of Science:

  • Epigenetics and chromatin biology
  • Molecular biology
  • Protein-biochemistry

Background:

  • Histone modifications are crucial for regulating chromatin structure and gene expression.
  • Understanding how proteins recognize specific histone modification patterns (the 'histone code') is essential for deciphering cellular processes.

Purpose of the Study:

  • To develop a novel combinatorial library of histone H4 N-terminal tail modifications.
  • To systematically investigate how proteins recognize and bind to specific histone modification patterns.
  • To determine the binding specificity of the human JMJD2A demethylase for histone H4 peptides.

Main Methods:

  • Construction of a large, randomized combinatorial library of histone H4 peptides (800 members) with various post-translational modifications.
  • On-bead screening of the library using antibodies and a histone-binding protein (hJMJD2A).
  • Validation of binding specificity using isothermal titration calorimetry (ITC).

Main Results:

  • The library successfully identified peptides with specific modifications, demonstrating its utility in binding assays.
  • Screening with an anti-phosphoserine antibody confirmed its specificity for S1 phosphorylation.
  • Analysis of hJMJD2A binding revealed that K20 methylation is the primary determinant, but neighboring phosphorylation and acetylation can modulate binding affinity.

Conclusions:

  • The developed combinatorial histone H4 library is a powerful tool for probing the 'histone code' and understanding histone modification recognition.
  • The study elucidated the binding determinants for the histone demethylase hJMJD2A, highlighting the combinatorial nature of histone code interpretation.
  • This approach is broadly applicable for characterizing the specificity of various histone-binding proteins.