Related Experiment Video
Updated: Jul 15, 2026
09:26
Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
Published on: March 26, 2017
Histone variants and complexes involved in their exchange.
Thomas Kusch1, Jerry L Workman
1Department of Biochemistry and Molecular Biology, Room #123A, Rutgers University, 604 Allison Road, Piscataway, NJ 08854, USA. TNK@stowers-institute.org
Sub-Cellular Biochemistry
|May 9, 2007
Summary
Histone variants, distinct from canonical histones, are crucial for epigenetic regulation and chromosomal architecture. Their dysregulation is linked to various diseases, highlighting their importance in cellular responses.
Area of Science:
- Molecular Biology
- Epigenetics
- Chromatin Biology
Background:
- Canonical histones form nucleosomes during DNA replication.
- Histone variants are incorporated into specific genomic regions throughout the cell cycle.
- Factors mediating histone variant deposition into specialized chromatin domains are increasingly recognized.
Purpose of the Study:
- To elucidate the mechanisms of targeted histone variant deposition.
- To understand the turnover and posttranslational modification of histone variants.
- To explore the role of histone variants and associated factors in epigenetic control.
Main Methods:
- Investigating histone variant-interacting proteins.
- Analyzing chromatin domains enriched for histone variants.
- Studying the dynamics of histone variant exchange.
Main Results:
- Histone variants associate with specific deposition factors.
- These factors facilitate targeted incorporation into specialized chromatin.
- Emerging evidence links histone variants to gene expression and cellular responses.
Conclusions:
- Histone variants and their exchange complexes are key regulators of chromosomal architecture.
- Deregulation of histone variants is implicated in diseases including cancer, infertility, and aging.
- Further research into histone variant mechanisms is critical for understanding health and disease.
Related Concept Videos
02:32Histone 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,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:32Histone 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,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:30Histone 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...
01:12The 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...
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...
02:10The 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.
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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...
The paradox
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02:25Spreading 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.
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