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Related Concept Videos

Histone Modification02:32

Histone Modification

13.1K
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...
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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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Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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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.
Writers
The writer...
8.2K
The Nucleosome01:19

The Nucleosome

1.3K
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...
1.3K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

880
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...
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Heterochromatin02:38

Heterochromatin

11.4K
The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at...
11.4K

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Updated: Jun 8, 2025

Expression Analysis of Mammalian Linker-histone Subtypes
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Expression Analysis of Mammalian Linker-histone Subtypes

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On the Hunt for the Histone Code.

Beatrix M Ueberheide1, Sahana Mollah2, Benjamin A Garcia3

  • 1Proteomics Laboratory, Division of Advanced Research Technologies, Department of Biochemistry and Molecular Pharmacology, New York University Langone Health Center, New York, New York, USA; Department of Neurology, New York University Langone Health Center, New York, New York, USA.

Molecular & Cellular Proteomics : MCP
|November 3, 2024
PubMed
Summary
This summary is machine-generated.

Mass spectrometry revolutionized histone post-translational modification (PTM) analysis, enabling new discoveries in epigenetics. Pioneering work by Don Hunt advanced histone PTM detection and quantification methods.

Keywords:
epigeneticshistonemass spectrometrypost-translational modificationsproteomics

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Author Spotlight: Enhanced Histone PTM Isomer Identification Through LC-TIMS-ToF MS/MS and PASEF
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Area of Science:

  • Epigenetics
  • Proteomics
  • Genomics

Background:

  • Chromatin, composed of DNA and histones, packages the genome.
  • Histone post-translational modifications (PTMs) regulate chromatin accessibility and gene expression.
  • Early histone PTM analysis relied on site-specific antibodies.

Purpose of the Study:

  • To highlight the transformative impact of mass spectrometry on histone PTM research.
  • To acknowledge Don Hunt's pioneering contributions to epigenetics.
  • To recount early advancements in histone PTM detection and quantification.

Main Methods:

  • Development of innovative mass spectrometry-based approaches for histone PTM analysis.
  • Discovery of novel histone modifications.
  • Establishment of methods for detecting and quantifying histone PTMs.

Main Results:

  • Significant expansion of known histone modifications.
  • Advancement of state-of-the-art proteomics techniques for epigenetics.
  • Facilitation of broader research in the epigenetics field.

Conclusions:

  • Mass spectrometry, pioneered by Don Hunt, fundamentally changed histone PTM research.
  • His work enabled numerous subsequent discoveries in epigenetics.
  • The described methods remain crucial in contemporary proteomics.