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Related Concept Videos

Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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 variants are also...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
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,...
Heterochromatin02:38

Heterochromatin

The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...

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HOX Loci Focused CRISPR/sgRNA Library Screening Identifying Critical CTCF Boundaries
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A conserved function for the H2A.Z C terminus.

Daniel Wratting1, Angela Thistlethwaite, Michael Harris

  • 1Faculty of Life Sciences, University of Manchester M13 9PT, United Kingdom.

The Journal of Biological Chemistry
|April 12, 2012
PubMed
Summary
This summary is machine-generated.

The C-terminal tail of histone H2A variant Z (H2A.Z) is crucial for its function in yeast. A similar truncated H2A.Z protein in humans suggests a conserved role in chromatin association.

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Mass Spectrometry Analysis to Identify Ubiquitylation of EYFP-tagged CENP-A (EYFP-CENP-A)
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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Biology

Background:

  • Histone H2A variants, like H2A.Z, diversify chromatin structure and function.
  • H2A.Z is an ancient, conserved variant regulating gene expression and DNA damage response.

Purpose of the Study:

  • To investigate the role of the C-terminal tail of H2A.Z in budding yeast.
  • To identify and characterize human H2A.Z splice isoforms with potential functional implications.

Main Methods:

  • Analysis of H2A.Z truncation mutants in yeast.
  • Identification and characterization of a novel human H2A.Z-2 splice isoform.

Main Results:

  • The unstructured C-terminal tail of H2A.Z is essential for its normal function in yeast.
  • A novel human H2A.Z-2 isoform encodes a C-terminally truncated protein, similar to yeast mutants.
  • Truncated H2A.Z forms in both species exhibit looser chromatin association compared to full-length H2A.Z.

Conclusions:

  • The H2A.Z C-terminal tail plays a conserved role in regulating H2A.Z association with nucleosomes.
  • This finding highlights a conserved mechanism for H2A.Z function across species.