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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.
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Histone Variants at the Centromere02:30

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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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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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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.
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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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Histone variants and epigenetics.

Steven Henikoff1, M Mitchell Smith2

  • 1Howard Hughes Medical Institute, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109-1024.

Cold Spring Harbor Perspectives in Biology
|January 7, 2015
PubMed
Summary
This summary is machine-generated.

Histone variants, which replace standard histones, are key to chromatin differentiation and epigenetic memory. Their unique deposition mechanisms are crucial for cellular processes and maintaining cell identity.

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Genetics

Background:

  • Histones are fundamental proteins that package DNA into nucleosomes.
  • Histone synthesis primarily occurs during S phase for replication-coupled deposition.
  • Histone variants offer a mechanism for chromatin differentiation independent of DNA replication.

Purpose of the Study:

  • To explore the roles of histone variants in chromatin differentiation.
  • To investigate the mechanisms of histone variant deposition.
  • To understand the contribution of histone variants to epigenetic memory.

Main Methods:

  • Comparative analysis of histone variant evolution and structure.
  • Studies on histone variant metabolism and deposition pathways.
  • Examination of histone variant functions in DNA repair and transcriptional regulation.

Main Results:

  • Histone variants are deposited independently of DNA replication.
  • Alternative deposition mechanisms establish and maintain epigenetic states.
  • Histone variants play critical roles in chromosome segregation and DNA repair.

Conclusions:

  • Histone variants are essential for fundamental chromatin differentiation.
  • Understanding histone variant dynamics is key to deciphering epigenetic memory.
  • Histone variants are integral to various cellular processes beyond DNA packaging.