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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...
The Nucleosome01:19

The Nucleosome

Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...
The Nucleosome02:33

The Nucleosome

DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...
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,...

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In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy
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A thermodynamic model for Nap1-histone interactions.

Andrew J Andrews1, Gregory Downing, Kitty Brown

  • 1Howard Hughes Medical Institute and Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870, USA.

The Journal of Biological Chemistry
|August 30, 2008
PubMed
Summary
This summary is machine-generated.

Yeast nucleosome assembly protein 1 (yNap1) binds histone complexes H2A/H2B and H3/H4 with low nanomolar affinity. This interaction is crucial for understanding chromatin dynamics and histone regulation.

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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Chromatin Biology

Background:

  • Yeast nucleosome assembly protein 1 (yNap1) is implicated in chromatin maintenance.
  • yNap1 is thought to regulate histone concentrations to facilitate histone exchange and nucleosome dynamics.
  • Understanding yNap1-histone interactions offers insights into chromatin thermodynamics.

Purpose of the Study:

  • To quantitatively characterize the affinity of yNap1 for core histones.
  • To elucidate the stoichiometry and binding interfaces of yNap1-histone complexes.
  • To investigate the roles of protein and histone tails in yNap1-histone binding.

Main Methods:

  • Development of quantitative assays to measure yNap1-histone binding affinity.
  • Biochemical analysis of yNap1 interaction with histone H2A/H2B and H3/H4 complexes.
  • Investigation of the contribution of yNap1 and histone tails to binding.

Main Results:

  • yNap1 binds H2A/H2B and H3/H4 histone complexes with low nanomolar affinity.
  • Each yNap1 dimer accommodates two histone fold dimers.
  • yNap1 tails enhance binding, while histone tails exert a mild repressive effect.
  • The (H3/H4)2 tetramer shows higher affinity for DNA than for yNap1.

Conclusions:

  • yNap1 exhibits significant affinity for histone dimers and tetramers, supporting its role in histone management.
  • The specific binding stoichiometry and the influence of protein/histone tails provide mechanistic details for yNap1 function.
  • The differential affinity for DNA versus yNap1 suggests distinct roles in chromatin assembly and remodeling.