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Related Concept Videos

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...
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...

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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
10:40

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

Dynamics and function of compact nucleosome arrays.

Michael G Poirier1, Eugene Oh, Hannah S Tims

  • 1Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois, USA.

Nature Structural & Molecular Biology
|August 25, 2009
PubMed
Summary

Chromatin fiber dynamics, even in compact states, allow DNA-processing enzymes access through spontaneous site exposure and protein-induced decompaction. This reveals how chromatin structure facilitates crucial cellular processes.

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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
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Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging

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

Background:

  • Eukaryotic DNA is packaged into chromatin, which can block essential enzymes.
  • The mechanisms by which chromatin structure accommodates DNA-processing enzymes remain largely unknown.

Purpose of the Study:

  • To investigate the conformational dynamics of nucleosome arrays.
  • To understand how chromatin structure changes to allow access for DNA-processing proteins.

Main Methods:

  • Construction of fluorescently labeled trinucleosome arrays.
  • Analysis of chromatin conformational dynamics using fluorescence resonance energy transfer (FRET).
  • Characterization of Mg2+-dependent folding and intermediate conformational states.

Main Results:

  • Nucleosome arrays exhibit reversible, Mg2+-dependent folding with two defined intermediate states.
  • Chromatin arrays are highly dynamic, with conformational fluctuations occurring from microsecond to second timescales.
  • Compact chromatin states permit DNA binding via site exposure, and protein binding can induce decompaction.

Conclusions:

  • Spontaneous chromatin fiber dynamics provide multiple mechanisms for DNA-processing protein complexes to access and act on DNA.
  • Chromatin's dynamic nature is crucial for regulating access to the genome.