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Related Concept Videos

Histone Modification02:32

Histone Modification

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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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Histone Modification02:32

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Spreading of Chromatin Modifications02:25

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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.
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The Nucleosome Core Particle01:12

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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.
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The Nucleosome Core Particle02:10

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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.
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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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Updated: Dec 9, 2025

Author Spotlight: Developing Acetyl-Click Assay for HAT1 Inhibitor Screening
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The Ada2/Ada3/Gcn5/Sgf29 histone acetyltransferase module.

Jose M Espinola-Lopez1, Song Tan1

  • 1Center for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.

Biochimica Et Biophysica Acta. Gene Regulatory Mechanisms
|September 5, 2020
PubMed
Summary
This summary is machine-generated.

Histone acetylation by Gcn5 (KAT2A) is crucial for gene regulation. This review details Gcn5

Keywords:
Epigenetic modificationGene regulationHistone crosstalksHistone modificationProtein isoformsTranscriptional regulation

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Gene Regulation

Background:

  • Histone post-translational modifications regulate eukaryotic gene expression.
  • Gcn5 (KAT2A) is a histone acetyltransferase catalyzing acetylation of histone H3 lysine residues.
  • Gcn5 functions within the SAGA transcriptional coactivator complex's HAT module, including Ada2, Ada3, and Sgf29 subunits.

Purpose of the Study:

  • To review biochemical and structural studies of Gcn5.
  • To highlight functional interactions between Gcn5 and its associated subunits (Ada2, Ada3, Sgf29).
  • To explore the role of Ada2 in modulating Gcn5 activity and its presence in variant HAT modules.

Main Methods:

  • Biochemical analyses of Gcn5's acyltransferase activities.
  • Structural studies elucidating Gcn5 mechanisms.
  • Investigation of crosstalk between histone H3 phosphorylation, methylation, and acetylation.

Main Results:

  • Mechanisms of Gcn5's acetyl- and other acyltransferase activities on histone substrates are elucidated.
  • Crosstalk between histone H3 phosphorylation, methylation, and acetylation is detailed.
  • Ada2's role in enhancing Gcn5 histone acetyltransferase activity is demonstrated.

Conclusions:

  • Gcn5's enzymatic activities and substrate interactions are well-characterized.
  • Ada2 significantly influences Gcn5 activity and is found in various SAGA-related complexes.
  • Understanding Gcn5-Ada2 interactions provides insights into epigenetic regulation.