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Related Concept Videos

Histone Modification02:32

Histone Modification

17.1K
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...
17.1K
Histone Modification02:32

Histone Modification

4.9K
4.9K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

9.9K
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...
9.9K
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

2.3K
Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
2.3K
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

15.2K
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...
15.2K

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Correction to: Leukemia inhibitory factor inhibits erythropoietin-induced myelin gene expression in oligodendrocytes.

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Leukemia inhibitory factor inhibits erythropoietin-induced myelin gene expression in oligodendrocytes.

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Related Experiment Video

Updated: Mar 24, 2026

Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models
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Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models

Published on: March 24, 2019

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Unwrapping Neurotrophic Cytokines and Histone Modification.

Cieron Roe1

  • 1Brighton and Sussex Medical School, The Audrey Emerton Building, Eastern Road, Kemp Town, Brighton, BN2 5BE, UK. c.roe1@uni.bsms.ac.uk.

Cellular and Molecular Neurobiology
|March 4, 2016
PubMed
Summary

Neuroinflammation

Area of Science:

  • Neuroscience
  • Immunology
  • Epigenetics

Background:

  • Neuroinflammation traditionally viewed as solely detrimental.
  • Pro-inflammatory cytokines like TNF-α play roles in axon regeneration and myelin repair.
  • Cytokine classification is evolving to 'neuroprotective' or 'neurosuppressive' properties.

Purpose of the Study:

  • To explore the role of cytokine-induced histone modification in oligodendrocyte differentiation.
  • To investigate the influence of intrinsic factors on axoglial regeneration outcomes.
  • To examine the potential of epigenetic targets in enhancing remyelination therapies.

Main Methods:

  • Review and commentary on existing literature.
  • Analysis of cytokine signaling pathways in neuroinflammation.
Keywords:
EpigeneticsHistone modificationMyelinationNeurodegenerationNeurotrophic cytokinesOligodendrocytesTherapy

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  • Exploration of epigenetic mechanisms (histone modification) in oligodendrocyte differentiation.

    • Main Results:

    • Neuroinflammation can release factors like leukaemia inhibitory factor (LIF) and erythropoietin (EPO) that promote oligodendrocyte differentiation and myelination.
    • Histone deacetylation is identified as a suppressor of oligodendrocyte differentiation inhibitors.
    • LIF and EPO may induce histone deacetylases, suggesting an epigenetic link.

    Conclusions:

    • Cytokine-induced histone modification is a critical intrinsic factor influencing oligodendrocyte differentiation and remyelination.
    • Epigenetic drug targets hold promise for potentiating exogenous cytokine therapy in neurological repair.
    • Future research should investigate the direct link between cytokine-induced histone deacetylases and remyelination outcomes.