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Related Concept Videos

Histone Modification02:32

Histone Modification

14.7K
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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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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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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Inheritance of Chromatin Structures03:17

Inheritance of Chromatin Structures

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Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
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The Nucleosome01:19

The Nucleosome

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Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...
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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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Extra-nuclear histones: origin, significance and perspectives.

Abhilasha Singh1, Sudhir Verma2, Sharmila Basu Modak1

  • 1Department of Zoology, University of Delhi, Delhi, 110007, India.

Molecular and Cellular Biochemistry
|November 19, 2021
PubMed
Summary

Histones, traditionally nuclear proteins, are found outside the cell nucleus. This study explores their formation, effects on membranes, and roles in extracellular vesicles and physiology.

Keywords:
Cytoplasmic histonesExosomal histonesExosomesExtra-nuclear histonesVesicle-associated histones

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Histones are primarily known for organizing DNA into chromatin within the eukaryotic nucleus.
  • Emerging evidence shows histones in the cytoplasm, circulation, and associated with extracellular vesicles.
  • The functions and formation mechanisms of these extra-nuclear histones are not fully understood.

Purpose of the Study:

  • To consolidate the mechanisms behind extra-nuclear histone formation.
  • To investigate the implications of histone-induced membrane destabilization.
  • To explore the association and release mechanisms of histones with extracellular vesicles and their physiological roles.

Main Methods:

  • Review and consolidation of existing scientific literature.
  • Analysis of proposed mechanisms for histone release and interaction.
  • Exploration of functional data regarding extra-nuclear histones.

Main Results:

  • Extra-nuclear histones can form through various mechanisms, interacting with cellular membranes due to charge properties.
  • Histone presence outside the nucleus can lead to membrane destabilization.
  • Histones are associated with extracellular vesicles, suggesting roles in intercellular communication.

Conclusions:

  • Extra-nuclear histones have diverse origins and functions beyond chromatin organization.
  • Understanding histone-membrane and histone-vesicle interactions is crucial for cell and systemic physiology.
  • Further research is needed to fully elucidate the significance of these extra-nuclear histones.