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Related Concept Videos

Histone Modification02:32

Histone Modification

15.4K
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...
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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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Heterochromatin02:38

Heterochromatin

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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at...
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Heterochromatin02:38

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Euchromatin01:01

Euchromatin

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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions take up more dye, appearing darker, while the less-compact areas take up less dye and appear lighter. Based on the compaction level, chromatins are classified into two primary forms – euchromatin and heterochromatin.
Euchromatin is the less dense region of the chromatin and stains lighter. Euchromatin contains histone H3 extensively...
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Related Experiment Video

Updated: Dec 9, 2025

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

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Histone H4-Specific Deacetylation at Active Coding Regions by Hda1C.

Min Kyung Lee1, TaeSoo Kim1

  • 1Department of Life Science and the Research Center for Cellular Homeostasis, Ewha Womans University, Seoul 03760, Korea.

Molecules and Cells
|September 11, 2020
PubMed
Summary

The Hda1 histone deacetylase complex (Hda1C) selectively deacetylates histones H4 and H3. This regulates RNA Polymerase II elongation and gene induction kinetics, revealing distinct roles in transcription.

Keywords:
Hda1Cgene inductionhistone deacetylationsubstrate switchingtranscription elongation

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Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Epigenetics

Background:

  • Histone acetylation and deacetylation are key regulators of chromatin structure and RNA Polymerase II (RNA Pol II) transcription.
  • The Hda1 histone deacetylase complex (Hda1C) is known to deacetylate histones H3 and H2B, repressing transcription.
  • Previous research suggested Hda1C might also deacetylate histone H4.

Purpose of the Study:

  • To review recent findings on transcriptional regulation by Hda1C-mediated histone deacetylation.
  • To explore the distinct roles of Hda1C in histone deacetylation and transcription.
  • To discuss potential mechanisms for Hda1C's histone substrate switching.

Main Methods:

  • Literature review of recent studies on Hda1C.
  • Analysis of Hda1C's roles in histone deacetylation and RNA Pol II transcription.
  • Investigation of factors influencing Hda1C substrate specificity.

Main Results:

  • Hda1C exhibits two distinct functions in histone deacetylation and transcription.
  • H4-specific deacetylation by Hda1C negatively regulates RNA Pol II elongation at highly transcribed genes.
  • H3 deacetylation by Hda1C fine-tunes gene induction kinetics upon environmental changes.

Conclusions:

  • Hda1C plays dual roles in gene regulation through differential histone deacetylation.
  • Transcriptional frequency and activity influence Hda1C's histone substrate preference.
  • Understanding Hda1C's mechanisms provides insights into epigenetic control of transcription.