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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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The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
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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.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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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
The writer...
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The Nucleosome01:19

The Nucleosome

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Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...
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Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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Updated: Aug 12, 2025

Author Spotlight: Epigenetic Modifications and Metabolic Rewiring as Targets for Cancer Therapy
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Author Spotlight: Epigenetic Modifications and Metabolic Rewiring as Targets for Cancer Therapy

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Nanoscale shape-dependent histone modifications.

Wei Zhang1,2, Jingji Li2, Camila P Silveira2

  • 1Guangdong Provincial Education Department Key Laboratory of Nano-Immunoregulation Tumor Microenvironment, The Second Affiliated Hospital, Guangzhou Medical University, Guangzhou 510260, Guangdong, P.R. China.

PNAS Nexus
|January 30, 2023
PubMed
Summary
This summary is machine-generated.

Nanoscale particle shape influences cellular epigenetics by inducing physical forces, impacting immune responses and potentially disease. This discovery opens new avenues for understanding immune regulation and memory.

Keywords:
bionanosynapseepigeneticsgold nanoparticlehistone modificationnanoscale shape

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Area of Science:

  • Nanotechnology
  • Immunology
  • Epigenetics
  • Cellular Biology

Background:

  • Complex nanoscale particulate shape is increasingly recognized for its role in regulating immune processes.
  • Cellular recognition of nanostructures may involve non-molecular inputs, such as physical forces.
  • Understanding these physical interactions is crucial for deciphering immune system behavior.

Purpose of the Study:

  • To investigate the impact of nanoscale particulate shape on cellular epigenetic modifications.
  • To explore the potential link between nanoscale forces and epigenetic regulation.
  • To examine the implications for immune regulation and disease.

Main Methods:

  • Utilized advanced nanoscale imaging and manipulation techniques.
  • Performed Chromatin Immunoprecipitation sequencing (ChIP-Seq) to analyze epigenetic marks.
  • Analyzed differential marking of H3K27me3 in response to nanoscale shape.

Main Results:

  • Demonstrated nanoscale shape-dependent control over the cellular epigenome.
  • Found that differential H3K27me3 marking correlates with nanoscale force sensing.
  • Identified a potential mechanism for immune cells to recognize and respond to physical cues from nanoparticles.

Conclusions:

  • Nanoscale particle shape can directly influence the cellular epigenome through physical force transduction.
  • Epigenetic modifications, specifically H3K27me3, are implicated in the cellular recognition of nanoscale forces.
  • These findings have significant implications for understanding particle-induced immune regulation, immune memory, and the development of immune-related diseases and their treatments.