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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,...
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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 variants are also...
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...
Inheritance of Chromatin Structures03:17

Inheritance of Chromatin Structures

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 DNA...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: Jun 25, 2026

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
10:09

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Published on: January 26, 2018

Histone H3 phosphorylation: universal code or lineage specific dialects?

Heriberto Cerutti1, J Armando Casas-Mollano

  • 1School of Biological Sciences and Center for Plant Science Innovation, University of Nebraska, Lincoln, NE 68588, USA. hcerutti1@unl.edu

Epigenetics
|February 27, 2009
PubMed
Summary

Histone H3 phosphorylation impacts gene expression and chromosome dynamics. Understanding these modifications requires deciphering organism-specific "histone codes" due to varied kinase evolution and functional differences.

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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
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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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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

Published on: May 17, 2016

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Biology

Background:

  • Post-translational modifications of histones, particularly phosphorylation, are crucial for regulating chromatin function and DNA-mediated processes.
  • Histone H3 phosphorylation is implicated in gene expression regulation and chromosome condensation/segregation during the cell cycle.
  • Conserved residues (Thr3, Ser10, Thr11, Ser28) on histone H3 are phosphorylated across diverse eukaryotes, yet the involved kinases and mechanisms show lineage-specific divergence.

Purpose of the Study:

  • To explore the evolutionary divergence of kinases responsible for histone H3 phosphorylation.
  • To investigate the varying mechanistic functions of specific phosphorylated histone H3 residues across eukaryotes.
  • To highlight the context-dependent nature of histone H3 phosphorylation marks, such as H3 Ser10 phosphorylation, in interpreting the 'histone code'.

Main Methods:

  • Comparative analysis of conserved histone H3 phosphorylation sites (Thr3, Ser10, Thr11, Ser28) across metazoa and plants.
  • Review of literature on kinase evolution and functional divergence related to histone H3 phosphorylation.
  • Examination of the combinatorial effects of histone modifications within specific chromatin contexts.

Main Results:

  • Kinases involved in histone H3 phosphorylation have evolved independently in different eukaryotic lineages.
  • The functional significance of specific phosphorylated amino acids on histone H3 varies among eukaryotes.
  • Histone H3 Ser10 phosphorylation exhibits context-dependent roles, acting both positively and negatively, and requires integration with other histone marks.

Conclusions:

  • A comprehensive understanding of histone H3 phosphorylation's biological impact necessitates appreciating organism-specific variations in the 'histone code'.
  • Future research should focus on deciphering these organismal dialects to fully elucidate chromatin regulation.