Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Nucleosome Remodeling02:54

Nucleosome Remodeling

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...
Histone Modification02:32

Histone Modification

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 deacetylase,...
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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 is an enzyme that can...
Histone Modification02:32

Histone Modification

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 deacetylase,...
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

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...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Antitumor efficacy of intermittent low-dose erlotinib plus sulindac via MHC upregulation and remodeling of the immune cell niche.

International journal of cancer·2025
Same author

Addressing barriers to global multidisciplinary stakeholder inclusivity: Lessons from global orofacial cleft research priority setting.

Journal of global health·2024
Same author

Alternative splicing of BAZ1A in colorectal cancer disrupts the DNA damage response and increases chemosensitization.

Cell death & disease·2024
Same author

Epigenetic regulation of major histocompatibility complexes in gastrointestinal malignancies and the potential for clinical interception.

Clinical epigenetics·2024
Same author

Erlotinib suppresses tumorigenesis in a mouse model of colitis-associated cancer.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie·2024
Same author

A-Z of Epigenetic Readers: Targeting Alternative Splicing and Histone Modification Variants in Cancer.

Cancers·2024

Related Experiment Video

Updated: Jun 24, 2026

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
11:02

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

Published on: May 17, 2016

Dietary manipulation of histone structure and function.

Barbara Delage1, Roderick H Dashwood

  • 1Linus Pauling Institute, Oregon State University, Corvallis, Oregon 97331-6512, USA.

Annual Review of Nutrition
|July 5, 2008
PubMed
Summary

Maternal nutrition influences fetal epigenetic programming through histone modifications, impacting long-term health and disease susceptibility. Dietary interventions may target these reversible epigenetic changes for cancer chemoprevention.

More Related Videos

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
09:43

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue

Published on: November 30, 2018

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
08:12

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

Published on: May 5, 2022

Related Experiment Videos

Last Updated: Jun 24, 2026

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
11:02

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

Published on: May 17, 2016

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
09:43

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue

Published on: November 30, 2018

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
08:12

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

Published on: May 5, 2022

Area of Science:

  • Epigenetics and Molecular Biology
  • Developmental Biology
  • Nutritional Science

Background:

  • Post-translational histone modifications are crucial regulators of chromatin structure, genomic stability, and gene expression.
  • Epigenetic programming during gametogenesis and fetal development has lasting effects on adult health.
  • Maternal nutrition is increasingly recognized as a significant factor influencing prenatal development and later-life disease susceptibility.

Purpose of the Study:

  • To investigate the role of histone modifications in mediating the effects of maternal nutrition on fetal development.
  • To explore the potential of dietary interventions in modulating epigenetic programming.
  • To understand the mechanisms by which maternal diet influences disease susceptibility through epigenetic alterations.

Main Methods:

  • Review of existing epidemiological and experimental studies on maternal nutrition and epigenetic modifications.
  • Analysis of histone modification patterns in relation to dietary intake during pregnancy.
  • Investigation of the impact of specific dietary components on histone-modifying enzymes.

Main Results:

  • Evidence suggests maternal diet can induce epigenetic alterations in histones during critical developmental periods.
  • These dietary-induced epigenetic changes may influence gene expression and chromatin structure.
  • Specific maternal dietary patterns are associated with altered disease susceptibility in offspring.

Conclusions:

  • Maternal nutrition plays a pivotal role in establishing epigenetic marks that influence long-term health outcomes.
  • Targeting histone modifications through diet represents a promising strategy for disease prevention and cancer chemoprevention.