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Related Concept Videos

Heterochromatin02:38

Heterochromatin

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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 that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at...
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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
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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.
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Nucleosome Remodeling02:54

Nucleosome Remodeling

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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.
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p300 forms a stable, template-committed complex with chromatin: role for the bromodomain.

E T Manning1, T Ikehara, T Ito

  • 1Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA.

Molecular and Cellular Biology
|May 22, 2001
PubMed
Summary

The coactivator p300 protein stably binds chromatin during transcription, with its bromodomain interacting with free histones, not nucleosomal ones. This interaction is crucial for p300 function in gene regulation.

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Gene Regulation

Background:

  • Understanding how coactivator proteins interact with active promoters in chromatin is key to transcriptional regulation.
  • The coactivator p300 plays a significant role in gene expression, but its precise interaction with chromatin is not fully understood.

Purpose of the Study:

  • To investigate the functional association of the coactivator p300 with chromatin templates.
  • To elucidate the role of the p300 bromodomain in chromatin binding and histone interactions.

Main Methods:

  • Biochemical assays, including in vitro transcription template competition assays.
  • Analysis of p300-chromatin complex formation and dependence on incubation time and activator proteins.
  • Examination of the binding properties of the isolated p300 bromodomain to free and nucleosomal histones.

Main Results:

  • p300 forms a stable, template-committed complex with chromatin during transcription, independent of activator proteins.
  • p300 directly binds to chromatin, requiring its bromodomain for this interaction.
  • The p300 bromodomain preferentially binds free histone H3 over nucleosomal histones.

Conclusions:

  • The stable association of p300 with chromatin is mediated, in part, by its bromodomain binding to histones.
  • This bromodomain-histone interaction is critical for p300 function in transcriptional regulation.
  • A model is proposed where p300 exhibits both activator-dependent targeting and activator-independent chromatin binding.