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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
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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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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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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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In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.

Andrew Bowman1, Colin M Hammond1, Andrew Stirling1

  • 1Centre for Gene Regulation and Expression, University of Dundee, Dundee, DD1 5EH, UK.

Nucleic Acids Research
|April 2, 2014
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Summary

Histone chaperones Vps75 and Nap1 form ring-shaped tetramers in solution, unlike their previously known dimeric form. This tetramerization may shield their surfaces when not carrying histones, acting as a self-chaperoning mechanism.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • NAP-1 fold histone chaperones are crucial for nucleosome assembly and disassembly.
  • Budding yeast Vps75 and Nap1 are known NAP-1 fold histone chaperones.
  • Previous studies crystallized Vps75 and Nap1 in homodimeric conformations.

Purpose of the Study:

  • To investigate the solution conformation of Vps75 and Nap1.
  • To determine if the dimeric conformation observed in crystals is maintained in solution.
  • To explore the functional implications of their solution structure.

Main Methods:

  • Small-angle X-ray scattering (SAXS)
  • Multi-angle light scattering (MALS)
  • Pulsed electron-electron double resonance (PELDOR)

Main Results:

  • Vps75 and Nap1 adopt ring-shaped tetrameric conformations in solution.
  • The tetrameric structure differs from the previously determined homodimeric crystal structure.
  • Homotetramerization appears to be a common feature of NAP-1 fold histone chaperones.

Conclusions:

  • NAP-1 fold histone chaperones can form tetramers in solution.
  • Tetramerization may serve as a 'self-chaperoning' mechanism by shielding acidic surfaces.
  • This structural flexibility is important for histone chaperone function.