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Related Concept Videos

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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Histone Modification02:32

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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

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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

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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.
The paradox
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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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Histone variants at a glance.

Paul B Talbert1, Steven Henikoff2

  • 1Howard Hughes Medical Institute, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue N, Seattle, WA 98109, USA ptalbert@fredhutch.org.

Journal of Cell Science
|March 27, 2021
PubMed
Summary
This summary is machine-generated.

Histone variants, which differ from standard histones, perform crucial roles throughout the cell cycle. Their unique structures influence nucleosome properties and specialized functions in DNA repair and gene regulation.

Keywords:
ChromatinEpigeneticsReplacement histones

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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
  • Genetics
  • Cell Biology

Background:

  • Eukaryotic chromatin is organized by nucleosomes, DNA wrapped around histone proteins.
  • Histone variants, unlike bulk histones, are available throughout the cell cycle and in post-mitotic cells.
  • These variants possess distinct structural features that impact nucleosome function.

Purpose of the Study:

  • To explore new insights into the evolutionary origins of histones.
  • To review histone variants from all major histone families.
  • To highlight how structural variations in histone variants influence their specialized functions.

Main Methods:

  • Literature review of recent findings on histone variants.
  • Analysis of structural differences among histone variants.
  • Discussion of functional implications of these structural variations.

Main Results:

  • Histone variants exhibit diverse structural properties, affecting DNA binding and nucleosome stability.
  • These structural differences correlate with specialized roles in DNA repair, chromosome segregation, and transcription.
  • Histone variants contribute to tissue-specific functions and cellular processes beyond S-phase.

Conclusions:

  • Histone variants are key regulators of chromatin structure and function.
  • Understanding histone variant structures is crucial for deciphering their diverse roles in cellular processes.
  • Further research into histone origins and variant functions will advance our knowledge of genome regulation.