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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,...
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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.
Writers
The writer is an enzyme that can...
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...
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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 variants are also...

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Related Experiment Video

Updated: Jul 2, 2026

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
11:02

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

Published on: May 17, 2016

Histone modifying enzymes: structures, mechanisms, and specificities.

Ronen Marmorstein1, Raymond C Trievel

  • 1Program in Gene Expression and Regulation, The Wistar Institute, Philadelphia, PA 19104, USA.

Biochimica Et Biophysica Acta
|August 30, 2008
PubMed
Summary
This summary is machine-generated.

Histone modifying enzymes control gene expression and cell fate through epigenetic modifications. This review highlights recent advances in understanding histone acetyltransferases and demethylases, posing key questions for future research.

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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
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Published on: August 1, 2017

Area of Science:

  • Biochemistry
  • Epigenetics
  • Molecular Biology

Background:

  • Histone modifying enzymes regulate gene expression and cell identity via epigenetic modifications.
  • These enzymes are crucial for maintaining the heritable epigenetic code.
  • Understanding their mechanisms provides insight into genomic functions.

Purpose of the Study:

  • To review recent advances in understanding histone modifying enzymes.
  • To highlight specific studies on histone acetyltransferases (HATs) and histone lysine demethylases (HDMs).
  • To identify overarching themes and outstanding questions regarding their regulatory roles in DNA transactions.

Main Methods:

  • Biochemical characterization of enzymes.
  • Structural characterization of enzymes.
  • Review of recent scientific literature.

Main Results:

  • Recent studies offer insights into the catalytic mechanisms, substrate specificities, and regulation of HATs (p300/KAT3B, Rtt109/KAT11) and HDMs (LSD1/KDM1, JMJD2A/KDM4A).
  • Overarching themes in enzyme regulation and function have emerged from these studies.
  • Key questions remain regarding their precise roles in mediating DNA transactions.

Conclusions:

  • Continued research into histone modifying enzymes is vital for understanding gene regulation and cell fate.
  • Further investigation is needed to fully elucidate the regulatory roles of these enzymes in DNA transactions.
  • The identified themes provide a framework for future research directions in epigenetics.