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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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Spreading of Chromatin Modifications02:25

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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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Inheritance of Chromatin Structures03:17

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Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
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Histone Modification02:32

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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
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In 1928, a German botanist Emil Heitz observed the moss nuclei with a DNA binding dye. He observed that while some chromatin regions decondense and spread out in the interphase nucleus, others do not. He termed them euchromatin and heterochromatin, respectively. He proposed that the heterochromatin regions reflect a functionally inactive state of the genome. It was later confirmed that heterochromatin is transcriptionally repressed, and euchromatin is transcriptionally active chromatin.
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Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers
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Defining the epichromatin epitope.

Travis J Gould1, Katalin Tóth2, Norbert Mücke2

  • 1a Department of Physics & Astronomy , Bates College , Lewiston , ME , USA.

Nucleus (Austin, Tex.)
|September 30, 2017
PubMed
Summary
This summary is machine-generated.

Epichromatin, identified by nucleosome antibodies, is located at the nuclear periphery during interphase and on mitotic chromosomes. Its structure and binding properties suggest roles in nuclear organization and reformation.

Keywords:
LANA (latency-associated nuclear antigen from Karposi's Sarcoma Herpesvirus)STEDacidic patchbivalent antibodychromomereconfocalmonovalent fab fragmentnucleosome

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Analysis of Histone Antibody Specificity with Peptide Microarrays
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Area of Science:

  • Cell Biology
  • Chromatin Biology
  • Immunocytochemistry

Background:

  • Epichromatin is a distinct chromatin structure identified by specific antibodies.
  • Its localization changes between interphase and mitosis.
  • Understanding epichromatin's structure and function is crucial for cell biology.

Purpose of the Study:

  • To characterize the structural and binding properties of epichromatin.
  • To investigate the epitope recognized by anti-nucleosome antibodies.
  • To explore the potential role of epichromatin in nuclear envelope reformation.

Main Methods:

  • Immunostaining with bivalent anti-nucleosome antibodies (PL2-6, 1H6) and monovalent Fab fragments.
  • STED microscopy for high-resolution imaging.
  • Co-immunostaining with anti-Ki-67.
  • Electrophoretic mobility shift assay (EMSA) and analytical ultracentrifugation.

Main Results:

  • Epichromatin thickness measured by STED microscopy (interphase ~76 nm, mitosis ~78 nm).
  • Distinct localization at the inner nuclear membrane (interphase) and outer surface of mitotic chromosomes.
  • Monovalent Fab fragments revealed a punctate, chromomeric staining pattern.
  • Antibody binding site suggests recognition of the nucleosome acidic patch.
  • Ki-67 found between epichromatin ridges during mitosis.

Conclusions:

  • Epichromatin exhibits distinct structural and localization patterns during the cell cycle.
  • The nucleosome acidic patch is likely part of the epichromatin epitope.
  • Differences in antibody binding suggest epitope accessibility varies between interphase and mitotic epichromatin.
  • Mitotic epichromatin's exposed surface may aid nuclear envelope reformation.