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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,...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...

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Related Experiment Video

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Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
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Structural cooperativity in histone H3 tail modifications.

Deniz Sanli1, Ozlem Keskin, Attila Gursoy

  • 1Department of Chemical and Biological Engineering, Koç University, 34450 Sariyer, Istanbul, Turkey.

Protein Science : a Publication of the Protein Society
|September 30, 2011
PubMed
Summary
This summary is machine-generated.

Histone H3 tail modifications at K4, K9, and K14 residues alter structural angles. These changes influence how histone modifying enzymes recognize and bind to the H3 tail, impacting cellular processes.

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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Post-translational modifications (PTMs) of histone H3 tails are critical regulators of cellular processes.
  • Cross-regulation exists between PTMs at lysine 4 (K4), K9, and K14 residues, significantly influencing each other's occurrence.

Purpose of the Study:

  • To investigate the structural consequences of key histone H3 tail modifications: K4 tri-methylation (K4me3), K9 tri-methylation (K9me3), and K14 acetylation (K14ace).
  • To analyze how these modifications affect backbone torsion angles and their implications for histone modifying enzyme recognition and binding.

Main Methods:

  • Extensive molecular dynamics simulations were performed on four distinct histone H3 tail constructs: unmodified, K4me3K9me3, K4me3K14ace, and K9me3K14ace.
  • Ramachandran plot analysis was employed to assess changes in dihedral angles (phi and psi) of key residues.

Main Results:

  • Tri-methylation of K4 significantly impacts its own dihedral angles, irrespective of other modifications.
  • K9 dihedral angles are notably altered, primarily influenced by K4 tri-methylation.
  • The phi and psi values of K14 are differentially affected by various combinations of K4/K9 methylation and K14 acetylation.

Conclusions:

  • Specific PTMs on histone H3 tails induce distinct structural changes in backbone torsion angles.
  • These structural alterations are crucial for the recognition and binding specificity of histone modifying enzymes, including DIM-5, GCN5, and JMJD2A.