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Related Concept Videos

Histone Modification02:32

Histone Modification

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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
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Covalently Linked Protein Regulators02:04

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Regulation of Expression at Multiple Steps01:23

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The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the...
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Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

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Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
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Co-activators and Co-repressors02:04

Co-activators and Co-repressors

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Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
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Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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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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Updated: Mar 15, 2026

Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers
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Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers

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CBP-IDRs regulate acetylation and gene expression.

Katie L Gelder1, Nicola A Carruthers1, Grace Gilbert2

  • 1Molecular and Cellular Biology, School of Biosciences, The University of Sheffield, Sheffield S10 2TN, UK; Nucleic Acids Institute, The University of Sheffield, Sheffield S10 2TN, UK.

Cell Reports
|March 13, 2026
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered regions (IDRs) in proteins like CBP cooperate to control nuclear functions. Their balance regulates gene expression, with disruption altering chromatin and acetylation patterns.

Keywords:
CBP/p300CP: molecular biologyIDPsIDRsacetylationbiomolecular condensateschromatinenhancersgene regulationintrinsically disordered proteinstranscription

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A Novel Bayesian Change-point Algorithm for Genome-wide Analysis of Diverse ChIPseq Data Types
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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Intrinsically disordered regions (IDRs) regulate protein function without stable structures.
  • IDRs are crucial in multidomain proteins like CBP and EP300, but their cooperative mechanisms are unclear.

Purpose of the Study:

  • To investigate how different IDRs within CBP cooperate to regulate complex nuclear behaviors.
  • To understand the balance between positive and negative regulatory interactions within CBP condensates.

Main Methods:

  • Analysis of CBP IDRs' sequence properties and their contribution to CBP behavior.
  • Assessment of CBP condensate regulation and sensitivity to lysine acetylation.
  • Evaluation of CBP's chromatin occupancy, histone acetylation, and gene expression.

Main Results:

  • Distinct CBP IDRs with varying sequence properties contribute uniquely to CBP function.
  • A critical balance between positive and negative regulatory interactions governs CBP condensates.
  • Disrupting this balance alters CBP's chromatin binding, histone acetylation, and gene expression.

Conclusions:

  • Different CBP IDRs exhibit intramolecular cooperation to control nuclear functions.
  • The properties of IDRs critically shape the functional landscape of multidomain proteins like CBP.