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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,...
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...
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...
Nucleosome Remodeling02:54

Nucleosome Remodeling

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.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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...

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Related Experiment Video

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Analysis of Histone Antibody Specificity with Peptide Microarrays
09:47

Analysis of Histone Antibody Specificity with Peptide Microarrays

Published on: August 1, 2017

JAK2 gets histone H3 rolling.

Martin Sattler1, James D Griffin

  • 1Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.

Cancer Cell
|November 3, 2009
PubMed
Summary
This summary is machine-generated.

Janus Kinase 2 (JAK2) activation plays a role in blood cell formation and cancer. This study shows JAK2-mediated histone H3 phosphorylation releases a gene repressor, enabling transcription.

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Last Updated: Jun 19, 2026

Analysis of Histone Antibody Specificity with Peptide Microarrays
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Published on: August 1, 2017

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
07:20

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Published on: October 18, 2024

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

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cancer Biology

Background:

  • Janus Kinase 2 (JAK2) activation is crucial for normal hematopoiesis (blood cell formation) and is frequently implicated in oncogenic transformations.
  • Understanding the precise molecular mechanisms by which JAK2 influences gene expression is vital for developing targeted therapies.

Purpose of the Study:

  • To elucidate the role of JAK2-mediated histone modifications in regulating gene transcription.
  • To investigate the interaction between JAK2, histone H3, and the heterochromatin protein 1 alpha (HP1alpha).

Main Methods:

  • The study employed biochemical assays and chromatin immunoprecipitation to analyze the effects of JAK2 activation on histone modifications.
  • Researchers investigated the release of HP1alpha from chromatin upon JAK2-mediated phosphorylation of histone H3.

Main Results:

  • Demonstrated that JAK2 directly phosphorylates histone H3.
  • Showed that this phosphorylation event leads to the dissociation of the transcriptional repressor HP1alpha from chromatin.
  • Observed that the release of HP1alpha results in the activation of specific gene transcription.

Conclusions:

  • JAK2-mediated phosphorylation of histone H3 is a key mechanism for releasing transcriptional repressors like HP1alpha.
  • This epigenetic regulation by JAK2 contributes to both normal hematopoiesis and potentially oncogenic processes.
  • The findings offer new insights into JAK2-driven gene expression and potential therapeutic targets.