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Related Concept Videos

Histone Modification02:32

Histone Modification

16.9K
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...
16.9K
Histone Modification02:32

Histone Modification

4.8K
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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 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...
5.2K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

2.6K
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...
2.6K
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

15.1K
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...
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Expression Analysis of Mammalian Linker-histone Subtypes
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Modulation of chromatin function through linker histone H1 variants.

Andrzej Kowalski1, Jan Pałyga1

  • 1Department of Biochemistry and Genetics, Institute of Biology, Jan Kochanowski University, 25-406 Kielce, Poland.

Biology of the Cell
|July 15, 2016
PubMed
Summary

Histone H1 variants

Keywords:
Chromatin structureHistone H1 variantsPolymorphismPosttranslational modificationsProtein dynamics

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Histone H1 proteins are crucial for chromatin organization.
  • Understanding their structure is key to their function.

Purpose of the Study:

  • To review the structural aspects of linker histone H1.
  • To characterize factors influencing H1 function in chromatin.

Main Methods:

  • Literature review of structural and functional studies.
  • Analysis of histone H1 variants, modifications, and diversification.

Main Results:

  • H1 histone variant function is dictated by dynamic tail domain alterations.
  • Posttranslational modifications and allelic diversification significantly impact H1 action.
  • Interdependent effects create dynamic H1 states influencing chromatin.

Conclusions:

  • Dynamic alterations in histone H1 structure, modifications, and variants are key to chromatin regulation.
  • These factors collectively influence chromatin organization and function.