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Related Concept Videos

Chromatin Structure Regulates pre-mRNA Processing02:41

Chromatin Structure Regulates pre-mRNA Processing

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In eukaryotic cells, nascent mRNA transcripts need to undergo many post-transcriptional modifications to reach the cell cytoplasm and translate into functional proteins. For a long time, transcription and pre-mRNA processing were considered two independent events that occur sequentially in the cell. However, it has now been well established that transcription and pre-mRNA processing are two simultaneous processes that are precisely regulated inside the cell.
The chromatin structure, especially...
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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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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.
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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.
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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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Related Experiment Video

Updated: Mar 26, 2026

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
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RNase P protein subunit Rpp29 represses histone H3.3 nucleosome deposition.

Alyshia Newhart1, Sara Lawrence Powers1, Prashanth Krishna Shastrula2

  • 1Molecular and Cellular Oncogenesis Program, Wistar Institute, Philadelphia, PA 19104.

Molecular Biology of the Cell
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Summary

Histone H3.3 deposition is regulated by RNA and involves RNase P. Rpp29 knockdown enhances H3.3 incorporation, impacting epigenetic regulation.

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Area of Science:

  • Epigenetics
  • Molecular Biology
  • Chromatin Biology

Background:

  • Histone H3.3 is crucial for transcription regulation and heritability.
  • The DAXX-ATRX-H3.3 pathway silences repetitive DNA, but pre-incorporation events are unclear.

Purpose of the Study:

  • To elucidate the events preceding H3.3 nucleosome incorporation.
  • To investigate the role of RNA and associated proteins in H3.3 deposition.

Main Methods:

  • Utilized a previously established inducible transgene system for visualization in single living cells.
  • Investigated the composition of the H3.3/RNA complex using knockdown experiments.

Main Results:

  • Identified nucleolar RNA proteins (Rpp29, fibrillarin, RPL23a) as components of the H3.3/RNA complex.
  • Demonstrated that Rpp29, a subunit of RNase P, represses H3.3 chromatin incorporation.
  • Showed that Rpp29 knockdown leads to increased H3.3 chromatin incorporation.

Conclusions:

  • Transcriptional events and associated RNA influence H3.3 recruitment and chromatin assembly.
  • A variant of RNase P appears to regulate H3.3 chromatin assembly.
  • Rpp29's repressive role in H3.3 deposition has significant implications for epigenetic regulation.