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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.
Writers
The writer...
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The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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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

The Nucleosome Core Particle

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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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Inheritance of Chromatin Structures03:17

Inheritance of Chromatin Structures

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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...
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Targeted in Situ Mutagenesis of Histone Genes in Budding Yeast
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Interrogating the function of metazoan histones using engineered gene clusters.

Daniel J McKay1, Stephen Klusza2, Taylor J R Penke3

  • 1Department of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Integrative Program for Biological and Genome Sciences, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Department of Genetics, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

Developmental Cell
|February 12, 2015
PubMed
Summary

Histone engineering in Drosophila reveals specific residue functions. H4K20 is not essential for development, while H3K36 is required for viability and H3K27 for cellular identity.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Developmental Biology

Background:

  • Histones and their posttranslational modifications regulate DNA-dependent processes.
  • Identifying individual histone residue functions is challenging due to non-histone targets of modifying enzymes and limited genetic engineering tools in metazoans.

Purpose of the Study:

  • To develop a platform in Drosophila for generating and analyzing any histone genotype.
  • To investigate the in vivo function of specific histone residues (H4K20, H3K36, H3K27).

Main Methods:

  • Development of a Drosophila platform for histone gene engineering.
  • Analysis of histone genotypes to assess effects on DNA replication, development, viability, and cellular identity.

Main Results:

  • Histone H4K20 is not essential for DNA replication or development.
  • Histone H3K36 is required for organismal viability.
  • Histone H3K27 is essential for maintaining cellular identity but not for gene activation.

Conclusions:

  • Histone engineering in Drosophila provides a powerful tool to study genome structure and function.
  • Specific histone residues have distinct roles in development, viability, and cellular identity.