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Related Concept Videos

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...
Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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 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...
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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 is an enzyme that can...

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In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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Published on: December 29, 2021

Expanded binding specificity of the human histone chaperone NASP.

Huanyu Wang1, Scott T R Walsh, Mark R Parthun

  • 1Department of Molecular and Cellular Biochemistry, The Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA.

Nucleic Acids Research
|September 11, 2008
PubMed
Summary

Nuclear autoantigenic sperm protein (NASP) binds both histone H1 and H3/H4. This study resolves conflicting reports, showing NASP functions as a versatile histone chaperone in chromatin assembly.

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Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

Area of Science:

  • Molecular biology
  • Chromatin biology
  • Protein biochemistry

Background:

  • Nuclear autoantigenic sperm protein (NASP) exhibits sequence similarity to H3/H4-specific histone chaperones.
  • Previous reports suggested NASP is an H1-specific histone chaperone, creating a paradox regarding its function.

Purpose of the Study:

  • To quantitatively analyze the binding specificity of human NASP.
  • To resolve the conflicting roles of NASP in histone chaperone activity.

Main Methods:

  • Native gel electrophoresis
  • Affinity chromatography assays
  • Surface plasmon resonance (SPR)
  • In vitro chromatin assembly assays

Main Results:

  • Human NASP binds histone H1 with high affinity.
  • Multiple experiments confirmed NASP forms distinct, high-specificity complexes with histones H3 and H4.
  • NASP demonstrated functional activity in H1-depleted chromatin assembly assays.

Conclusions:

  • NASP functions as a dual-specificity histone chaperone, interacting with both H1 and H3/H4.
  • The findings clarify NASP's role in chromatin assembly, accommodating its sequence homology and observed binding patterns.