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Related Concept Videos

Histone Modification02:32

Histone Modification

16.2K
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 Modification02:32

Histone Modification

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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...
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Chromosome Replication02:31

Chromosome Replication

10.8K
Before a cell can divide, it must accurately replicate all of its chromosomes, including the DNA and its associated histone and non-histone proteins.  This process begins at numerous origins of replication during the S phase of the cell cycle in each of a cell’s chromosomes simultaneously. Certain nucleotides can act as origins of replication, but these sequences are not well defined - especially in complex, multi-cellular, eukaryotic species. The length of DNA that spans an origin...
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Nucleosome Remodeling02:54

Nucleosome Remodeling

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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...
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Related Experiment Video

Updated: Feb 10, 2026

Analysis of Histone Antibody Specificity with Peptide Microarrays
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Analysis of Histone Antibody Specificity with Peptide Microarrays

Published on: August 1, 2017

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A histone reader becomes the readout.

Catherine A Musselman1, Tatiana G Kutateladze2

  • 1Department of Biochemistry, University of Iowa College of Medicine, Iowa City, Iowa 52242.

The Journal of Biological Chemistry
|May 13, 2018
PubMed
Summary

Researchers found that the oncoprotein TRIM24 is modified by SUMOylation when linked to specific histone marks. This process regulates genes involved in cell adhesion, offering new cancer drug development insights.

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cancer Research

Background:

  • Chromatin signaling regulates genome dynamics.
  • Histone modifications are well-studied, but nonhistone regulator modifications and cross-talk are less understood.

Purpose of the Study:

  • To investigate the modification and function of the transcription co-factor TRIM24.
  • To explore the relationship between TRIM24 modification and histone modifications.

Main Methods:

  • The study focused on TRIM24 (tripartite motif-containing protein 24) and its SUMOylation.
  • Investigated the association of TRIM24 with specific histone modification signatures.

Main Results:

  • TRIM24 undergoes SUMOylation upon binding to a specific histone modification signature.
  • This SUMOylation event regulates the transcription of genes associated with cell adhesion.

Conclusions:

  • Demonstrates a novel signaling pathway involving TRIM24 modification and chromatin regulation.
  • Provides insights into nuclear signaling cascades and potential targets for cancer drug development.