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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,...
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...
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

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...
Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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...

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Related Experiment Video

Updated: May 31, 2026

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
11:02

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

Histone modifications influence mediator interactions with chromatin.

Xuefeng Zhu1, Yongqiang Zhang, Gudrun Bjornsdottir

  • 1Department of Biochemistry and Cell Biology, University of Gothenburg, SE-405 30 Gothenburg, Sweden.

Nucleic Acids Research
|July 12, 2011
PubMed
Summary
This summary is machine-generated.

Mediator complex localization to DNA is guided by histone tails. Acetylation of histone H4 lysine 16 specifically inhibits this interaction, impacting gene transcription regulation.

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

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Chromatin Immunoprecipitation (ChIP) of Histone Modifications from Saccharomyces cerevisiae
11:06

Chromatin Immunoprecipitation (ChIP) of Histone Modifications from Saccharomyces cerevisiae

Published on: December 29, 2017

Related Experiment Videos

Last Updated: May 31, 2026

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
11:02

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

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

Chromatin Immunoprecipitation (ChIP) of Histone Modifications from Saccharomyces cerevisiae
11:06

Chromatin Immunoprecipitation (ChIP) of Histone Modifications from Saccharomyces cerevisiae

Published on: December 29, 2017

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Gene Regulation

Background:

  • The Mediator complex is crucial for gene transcription, bridging transcription factors and the core machinery.
  • Mediator complex occupancy is observed at both actively transcribed and silenced genomic regions.
  • Understanding Mediator localization is key to deciphering gene expression control.

Purpose of the Study:

  • To investigate the role of chromatin structure and histone modifications in guiding Mediator complex localization.
  • To elucidate the specific interactions between Mediator and histone tails.
  • To determine how post-translational modifications of histones affect Mediator binding.

Main Methods:

  • Quantitative genetic interaction mapping to identify factors influencing Mediator localization.
  • Peptide binding assays to assess direct interactions between Mediator and histone tails.
  • Tiling array analysis to examine in vivo Mediator and nucleosome occupancy.

Main Results:

  • Genetic mapping revealed links between Mediator and chromatin-modifying factors, including histone deacetylases.
  • Mediator directly binds to Histone H3 and H4 tails.
  • Histone H4 acetylation at lysine 16 specifically disrupts Mediator binding to histone H4 peptides.
  • In vivo studies showed a correlation between Mediator and nucleosome occupancy, but an inverse correlation with H4K16 acetylation.

Conclusions:

  • Chromatin structure, particularly histone tail modifications, plays a critical role in directing Mediator complex localization.
  • Histone H4 acetylation at lysine 16 acts as a specific regulator of Mediator-histone interactions.
  • These findings reveal a direct link between epigenetic modifications and the recruitment of the transcriptional machinery.