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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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No description available
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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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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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Covalently Linked Protein Regulators02:04

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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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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Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions.

Alexander J Ruthenburg1, Haitao Li, Thomas A Milne

  • 1Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University, 1230 York Avenue, New York, NY, 10065, USA.

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|May 21, 2011
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Summary

Combinations of histone modifications are key to chromatin function. This study identifies a specific pattern of histone marks (H3K4me3 and H4K16ac) that directs protein binding to nucleosomes.

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Area of Science:

  • Chromatin biology
  • Molecular epigenetics
  • Protein-DNA interactions

Background:

  • Histone modifications regulate gene expression and chromatin structure.
  • The BPTF protein's PHD finger recognizes methylated histone H3 (H3K4me2/3).
  • How combined histone marks influence protein binding at the nucleosome level is largely unknown.

Purpose of the Study:

  • To investigate how additional histone modifications affect BPTF binding.
  • To identify specific histone mark combinations recognized by BPTF.
  • To understand the role of nucleosomal mark patterning in chromatin associations.

Main Methods:

  • Systematic screening of peptide surrogates.
  • Biophysical characterization of protein-ligand interactions.
  • Mononucleosome binding assays.
  • Genome-wide colocalization analysis.

Main Results:

  • A PHD-adjacent bromodomain in BPTF was identified to bind three acetyllysine peptides.
  • The BPTF bromodomain showed selectivity for H4K16ac only when combined with H3K4me3 at the mononucleosome level.
  • This H3K4me3 and H4K16ac pattern was confirmed as a unique trans-histone modification within single nucleosomes in human cells.
  • This specific histone mark module colocalizes with BPTF binding sites in the genome.

Conclusions:

  • Nucleosomal patterning of covalent marks dictates critical chromatin associations.
  • The combination of H3K4me3 and H4K16ac on a single nucleosome is a specific recognition signal for BPTF.
  • This finding highlights the importance of considering the interplay of multiple histone marks for understanding chromatin regulation.