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Related Concept Videos

Histone Modification02:32

Histone Modification

16.8K
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

18.9K
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...
18.9K
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

2.3K
Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
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The Nucleosome Core Particle01:12

The Nucleosome Core Particle

2.6K
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.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
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Related Experiment Video

Updated: Mar 8, 2026

Assays for Validating Histone Acetyltransferase Inhibitors
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Targeting Class I Histone Deacetylases in a "Complex" Environment.

Christopher J Millard1, Peter J Watson1, Louise Fairall1

  • 1Henry Wellcome Laboratories of Structural Biology, Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 9HN, UK.

Trends in Pharmacological Sciences
|February 1, 2017
PubMed
Summary

Histone deacetylase (HDAC) inhibitors show promise for cancer and other diseases. Targeting specific HDAC complexes, rather than individual enzymes, may overcome current limitations in inhibitor selectivity and efficacy.

Keywords:
HDAC inhibitorsco-repressor complexesgene regulationhistone deacetylasesinositol phosphatestranscription repression

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Molecular Biology

Background:

  • Histone deacetylase (HDAC) inhibitors are established anticancer agents with therapeutic potential for HIV, Alzheimer's disease, and Friedreich's ataxia.
  • Current HDAC inhibitors lack specificity, targeting multiple deacetylases due to similar active site structures, posing a challenge for drug design.
  • HDACs 1, 2, and 3 are components of distinct multi-subunit complexes with specific biological roles.

Purpose of the Study:

  • To review structural information on HDAC complexes.
  • To discuss strategies for developing isoform-selective HDAC inhibitors by targeting these complexes.
  • To explore potential therapeutic applications of targeted HDAC inhibition.

Main Methods:

  • Literature review of structural and functional data on HDAC complex assembly.
  • Analysis of structural similarities and differences in HDAC active sites.
  • Discussion of potential targeting strategies for specific HDAC complexes.

Main Results:

  • HDACs 1, 2, and 3 participate in distinct multi-subunit complexes.
  • Structural and functional data on complex assembly offer opportunities for targeted inhibition.
  • Targeting complexes presents a viable strategy to achieve isoform selectivity.

Conclusions:

  • Targeting multi-subunit HDAC complexes offers a promising approach to enhance inhibitor selectivity.
  • Understanding complex assembly is crucial for designing novel HDAC-targeted therapeutics.
  • This strategy could lead to more effective treatments for cancer and other HDAC-related diseases.