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Related Concept Videos

Euchromatin01:01

Euchromatin

8.7K
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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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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Negative Regulator Molecules01:23

Negative Regulator Molecules

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Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.
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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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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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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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Related Experiment Video

Updated: Jan 5, 2026

Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers
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Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers

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E3 ligase RCHY1 negatively regulates HDAC2.

Mina Choi1, Yeong Min Choi2, In-Sook An2

  • 1Research Institute for Molecular-Targeted Drugs, Department of Cosmetics Engineering, Konkuk University, Seoul, 05029, South Korea.

Biochemical and Biophysical Research Communications
|October 22, 2019
PubMed
Summary

The E3 ligase RCHY1 negatively regulates Histone Deacetylase 2 (HDAC2) levels in cancer cells. This discovery reveals a new mechanism for controlling HDAC2, a target in cancer therapeutics.

Keywords:
HDAC2Protein degradationRCHY1

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Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
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Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cancer Research

Background:

  • Histone Deacetylase 2 (HDAC2), a class I histone deacetylase, regulates the epigenetic landscape via histone modification.
  • Overexpression of HDAC2 is observed in numerous cancers, driving the development of HDAC2-targeted cancer therapeutics.

Purpose of the Study:

  • To elucidate a novel regulatory mechanism for HDAC2.
  • To investigate the role of the E3 ligase RCHY1 in controlling HDAC2 expression and function.

Main Methods:

  • Meta-analysis of six independent tumor tissue datasets to assess the correlation between RCHY1 and HDAC2 levels.
  • In vitro experiments involving ectopic expression and knockdown of RCHY1 in various cancer cell lines (p53 wildtype, mutant, and null).
  • Co-immunoprecipitation assays to determine direct interaction between RCHY1 and HDAC2.

Main Results:

  • A significant inverse correlation was identified between RCHY1 and HDAC2 levels in tumor tissues across multiple datasets.
  • Ectopic expression of RCHY1 led to decreased HDAC2 levels in cancer cells, while RCHY1 knockdown resulted in increased HDAC2 levels.
  • Direct physical interaction between RCHY1 and HDAC2 was confirmed, with the RING domain of RCHY1 being crucial for this interaction and subsequent HDAC2 regulation.

Conclusions:

  • RCHY1 acts as a negative regulator of HDAC2.
  • The findings present a novel mechanism of HDAC2 regulation mediated by the E3 ligase RCHY1.
  • This regulatory axis may offer new therapeutic strategies targeting HDAC2 in cancer.