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Related Concept Videos

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 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...
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...
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...

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In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

Histone chaperone FACT coordinates nucleosome interaction through multiple synergistic binding events.

Duane D Winkler1, Uma M Muthurajan1, Aaron R Hieb1

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

The Journal of Biological Chemistry
|October 5, 2011
PubMed
Summary

The histone chaperone FACT binds DNA, histones, and nucleosomes with high affinity. Its Spt16 subunit displaces DNA, facilitating chromatin reorganization for DNA maintenance.

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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

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In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Dynamics

Background:

  • DNA maintenance in eukaryotic cells relies on chromatin template disassembly and reassembly.
  • Chromatin remodelers and histone chaperones are crucial extrinsic factors for these processes.
  • The histone chaperone FACT (facilitates chromatin transcription) plays key roles in transcription, replication, and repair by reorganizing nucleosomes.

Purpose of the Study:

  • To quantitatively assess the critical contacts mediating FACT function.
  • To elucidate the binding affinities of FACT to histones, DNA, and nucleosomes.
  • To determine the role of histone tails and the Spt16 subunit in FACT-mediated chromatin interactions.

Main Methods:

  • Quantitative binding assays to determine FACT's affinity for histones, DNA, and nucleosomes.
  • Experiments investigating the role of histone tails in FACT binding.
  • Analysis of the FACT subunit Spt16's acidic C-terminal domain function.
  • Studies using tri-nucleosome arrays to model FACT binding within chromatin.

Main Results:

  • FACT exhibits nanomolar binding concentrations for histones, DNA, and nucleosomes.
  • Histone tails are critical for FACT's interaction with free histones and nucleosomes.
  • The acidic C-terminal domain of Spt16 actively displaces nucleosomal DNA.
  • FACT binding within chromatin involves synchronized interactions with nucleosomal targets.

Conclusions:

  • Specific FACT subunits coordinate interactions with nucleosomal sites for high-affinity binding.
  • FACT binding promotes nucleosome reorganization essential for DNA maintenance processes.
  • The study provides a quantitative understanding of FACT's mechanism in chromatin dynamics.