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Related Concept Videos

Histone Modification02:32

Histone Modification

14.4K
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...
14.4K
Histone Modification02:32

Histone Modification

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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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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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Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

1.5K
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...
1.5K
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...
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Related Experiment Video

Updated: Apr 23, 2026

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue

Published on: November 30, 2018

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Can changes in histone acetylation contribute to memory formation?

Jose P Lopez-Atalaya1, Angel Barco1

  • 1Instituto de Neurociencias, Universidad Miguel Hernández-Consejo Superior de Investigaciones Científicas, Av. Santiago Ramón y Cajal s/n. Sant Joan d'Alacant, 03550 Alicante, Spain.

Trends in Genetics : TIG
|October 2, 2014
PubMed
Summary

Histone acetylation in neurons is debated as a memory mechanism. Further research must distinguish epigenetic causes from effects in neuronal plasticity and memory.

Keywords:
HDACiactivity-driven transcriptionepigeneticshistone acetylationhistone codelearning and memorytranscriptional regulation

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Area of Science:

  • Neuroscience
  • Epigenetics
  • Molecular Biology

Background:

  • Neuronal histone acetylation is proposed as a substrate for memory formation.
  • It is also considered a target for memory-enhancing and neuropsychiatric drugs.

Purpose of the Study:

  • Critically evaluate the role of neuronal histone acetylation in memory.
  • Examine conflicts between proposed roles and genomic/genetic evidence.
  • Discuss alternative interpretations of existing data.

Main Methods:

  • Literature review and critical analysis of existing studies.
  • Examination of genomic and genetic data from various systems.
  • Debate on the interpretation of activity-dependent neuronal histone acetylation.

Main Results:

  • The proposed instructive role of histone acetylation in memory-related transcription faces challenges.
  • Insights from other systems suggest a complex interplay of epigenetic mechanisms.
  • Current evidence allows for alternative interpretations beyond classical transcriptional roles.

Conclusions:

  • Distinguishing cause from effect is crucial for understanding epigenetic modifications in neuronal plasticity and memory.
  • Further progress requires differentiating novel epigenetics-related processes from classical transcriptional mechanisms.
  • Clarifying the role of histone acetylation is essential for advancing research in memory and neuropsychiatric disorders.