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Related Concept Videos

Chromatin Immunoprecipitation- ChIP02:36

Chromatin Immunoprecipitation- ChIP

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Chromatin immunoprecipitation, or ChIP, is an antibody-based technique used to identify sites on DNA that bind to transcription factors of interest or histone proteins. It also helps determine the type of histone modifications such as acetylation, phosphorylation, or methylation.
Types of ChIP
ChIP can be divided into two types - X-ChIP and N-ChIP. X-ChIP involves in vivo cross-linking of histones and regulatory proteins to DNA, fragmenting the DNA by sonication, and isolating the protein-DNA...
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Euchromatin01:01

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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions take up more dye, appearing darker, while the less-compact areas take up less dye and appear lighter. Based on the compaction level, chromatins are classified into two primary forms – euchromatin and heterochromatin.
Euchromatin is the less dense region of the chromatin and stains lighter. Euchromatin contains histone H3 extensively...
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Chromatin Position Affects Gene Expression02:35

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Chromatin is the massive complex of DNA and proteins packaged inside the nucleus. The complexity of chromatin folding and how it is packaged inside the nucleus greatly influences  access to genetic information. Generally, the nucleus' periphery is considered transcriptionally repressive, while the cell's interior is considered a transcriptionally active area. 
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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...
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Chromatin Packaging02:21

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Each human somatic cell contains 6 billion base-pairs of DNA. Each base-pair is 0.34 nm long, which means that each diploid cell contains a staggering 2 meters of DNA. How is such a long DNA strand packed inside a nucleus measuring only 10 - 20 microns in diameter? 
The chromatin
In combination with specialized DNA binding protein called Histones, the DNA double helix forms a compact DNA: protein complex called chromatin. The chromatin itself is further compacted into higher-order...
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Chromatin Packaging01:32

Chromatin Packaging

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Each human somatic cell contains 6 billion base pairs of DNA. Each base pair is 0.34 nm long, meaning each diploid cell contains a staggering 2 meters of DNA. This long DNA strand is packed inside a nucleus measuring only 10-20 microns in diameter with the help of specialized DNA-binding proteins called histones. Together they form a compact DNA-protein complex called chromatin. The chromatin is further compacted into higher-order structures. The highest level of compaction is achieved during...
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Immunostaining for DNA Modifications: Computational Analysis of Confocal Images
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Visualizing Chromatin Modifications in Isolated Nuclei.

Yuan Li1, Zachary Klase2, Luca Sardo1

  • 1Department of Infectious Diseases and Vaccines, MRL, Merck & Co. Inc., West Point, PA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|July 19, 2020
PubMed
Summary

Researchers developed a new microscopy method to observe real-time changes in chromatin structure within live cells. This technique allows for the visualization of drug effects on nuclear architecture in living cells.

Keywords:
AcetylationChromatinHistoneMicroscopyNucleus

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Traditional chromatin structure analysis relies on biochemical assays yielding population averages.
  • Microscopy offers single-cell resolution but often requires fixed samples or exogenous proteins.
  • Observing dynamic chromatin changes in real-time within live cells remains a challenge.

Purpose of the Study:

  • To develop a novel microscopy technique for observing dynamic chromatin structure modifications in live cells.
  • To enable real-time visualization of endogenous protein behavior related to chromatin.
  • To assess the impact of pharmacological agents on nuclear architecture in living cells.

Main Methods:

  • Isolation of transcriptionally and enzymatically active nuclei from live cells.
  • Utilization of fluorescently labeled antibodies for visualizing endogenous nuclear proteins.
  • Real-time microscopic observation of nuclear events and chromatin dynamics.

Main Results:

  • Successful isolation and real-time imaging of active nuclei from live cells.
  • Demonstration of visualizing dynamic changes in chromatin architecture.
  • Capability to observe the effects of drugs on nuclear morphology and chromatin structure under microscopic observation.

Conclusions:

  • The developed method allows for real-time observation of chromatin dynamics in live cells.
  • This technique provides a powerful tool for studying nuclear architecture and drug effects.
  • It overcomes limitations of traditional biochemical assays and fixed-sample microscopy.