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Related Concept Videos

Histone Modification02:32

Histone Modification

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 deacetylase,...
Histone Modification02:32

Histone Modification

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 deacetylase,...
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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 is an enzyme that can...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Related Experiment Video

Updated: Jun 19, 2026

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
09:43

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

Published on: November 30, 2018

Protein phosphatase 1 regulates the histone code for long-term memory.

Kyoko Koshibu1, Johannes Gräff, Monique Beullens

  • 1Brain Research Institute, University of Zürich, Swiss Federal Institute of Technology, CH-8057 Zurich, Switzerland.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
|October 16, 2009
PubMed
Summary

Protein phosphatase 1 (PP1) regulates brain chromatin remodeling, controlling histone modifications and gene transcription essential for long-term memory formation in mammals.

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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
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Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
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Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Published on: January 26, 2018

Area of Science:

  • Neuroscience
  • Epigenetics
  • Molecular Biology

Background:

  • Epigenetic regulation via histone posttranslational modifications (PTMs) and DNA methylation influences cognitive functions.
  • Mechanisms underlying epigenetic control of memory remain largely unknown.

Purpose of the Study:

  • To investigate the role of protein phosphatase 1 (PP1) in regulating chromatin remodeling and gene transcription in the mammalian brain.
  • To elucidate the involvement of PP1 in the epigenetic mechanisms underlying long-term memory.

Main Methods:

  • Investigated PP1 localization and interactions with epigenetic enzymes (HDAC1, JMJD2A) in brain chromatin.
  • Utilized transgenic mice with selective inhibition of nuclear PP1 in forebrain neurons.
  • Analyzed residue-specific histone PTMs, gene promoter activity, RNA polymerase II binding, and gene transcription.

Main Results:

  • PP1 is present in brain cell chromatin and interacts with histone deacetylase 1 (HDAC1) and jumonji domain-containing protein 2A (JMJD2A).
  • Inhibition of nuclear PP1 in forebrain neurons induced specific histone PTMs (phosphorylation, acetylation, methylation) at memory-related gene promoters (CREB, NF-kappaB).
  • These epigenetic changes correlated with altered gene transcription, RNA polymerase II binding, and enhanced long-term memory for objects and space.

Conclusions:

  • PP1 is a critical regulator of chromatin remodeling in the mammalian brain.
  • PP1 controls histone PTMs and gene transcription pathways crucial for long-term memory.
  • This study reveals a novel PP1-dependent epigenetic mechanism for regulating gene transcription and memory in the adult brain.