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Related Concept Videos

Histone Modification02:32

Histone Modification

15.4K
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...
15.4K
Histone Modification02:32

Histone Modification

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4.1K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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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.
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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The Nucleosome Core Particle02:10

The Nucleosome Core Particle

13.7K
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...
13.7K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

9.1K
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...
9.1K
Heterochromatin02:38

Heterochromatin

17.2K
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...
17.2K

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Updated: Dec 10, 2025

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
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Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

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Interactions With Histone H3 & Tools to Study Them.

William A Scott1,2, Eric I Campos1,2

  • 1Genetics & Genome Biology Program, The Hospital for Sick Children, Toronto, ON, Canada.

Frontiers in Cell and Developmental Biology
|August 28, 2020
PubMed
Summary
This summary is machine-generated.

Histone proteins H3.1 and H3.3 dynamically change during the cell cycle, influenced by chaperones and modifications. New tools help study these dynamic histone-protein interactions in chromatin.

Keywords:
H3.1H3.3chromatinepigenetichistonenucleosomeproteomic

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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
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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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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
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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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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cell Biology

Background:

  • Histones are key components of chromatin, regulating its structure, dynamics, and function.
  • Histone variants, posttranslational modifications, and binding proteins significantly impact chromatin.
  • Nucleosomal histones undergo dynamic changes throughout the cell cycle, including transcription and replication.

Purpose of the Study:

  • To provide an overview of H3.1 and H3.3 histone dynamics during the cell cycle.
  • To highlight tools for studying dynamic histone-protein interactions.
  • To discuss histone chaperoning, modification, and binding events.

Main Methods:

  • Review of established and emerging technologies for studying chromatin dynamics.
  • Focus on experimental tools for spatiotemporal chromatin analysis.
  • Emphasis on methods investigating histone chaperones, modifications, and effector proteins.

Main Results:

  • Histones H3.1 and H3.3 exhibit distinct dynamic behaviors across the cell cycle.
  • Various proteins chaperone, modify, and bind histones at different cell cycle stages.
  • Evolving technologies enhance the understanding of dynamic histone-protein interactions.

Conclusions:

  • Understanding histone dynamics is crucial for comprehending chromatin regulation.
  • Advanced tools are essential for dissecting complex histone-protein interactions.
  • Further research using these technologies will illuminate chromatin functions.