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

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 Variants at the Centromere02:30

Histone Variants at the Centromere

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 variants are also...
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,...
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,...
Epigenetic Regulation01:37

Epigenetic Regulation

Epigenetic changes alter the physical structure of the DNA without changing the genetic sequence and often regulate whether genes are turned on or off. This regulation ensures that each cell produces only proteins necessary for its function. For example, proteins that promote bone growth are not produced in muscle cells. Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
X-chromosome...
Epigenetic Regulation01:46

Epigenetic Regulation

Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.

You might also read

Related Articles

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

Sort by
Same author

Deliberating performance targets workshop: Potential paths for emerging PM<sub>2.5</sub> and O<sub>3</sub> air sensor progress.

Atmospheric Environment: X·2021
Same author

Preparation and Biochemical Analysis of Classical Histone Deacetylases.

Methods in enzymology·2016
Same author

Targeting histone deacetylase 6 mediates a dual anti-melanoma effect: Enhanced antitumor immunity and impaired cell proliferation.

Molecular oncology·2015
Same author

Deacetylation of the tumor suppressor protein PML regulates hydrogen peroxide-induced cell death.

Cell death & disease·2014
Same author

Epstein-Barr virus maintains lymphomas via its miRNAs.

Oncogene·2013
Same author

Myc represses miR-15a/miR-16-1 expression through recruitment of HDAC3 in mantle cell and other non-Hodgkin B-cell lymphomas.

Oncogene·2011

Related Experiment Video

Updated: Jul 13, 2026

Assays for Validating Histone Acetyltransferase Inhibitors
09:11

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

Histone deacetylases and cancer.

M A Glozak1, E Seto

  • 1H. Lee Moffitt Cancer Center & Research Institute, Tampa, FL, USA.

Oncogene
|August 19, 2007
PubMed
Summary

Histone deacetylases (HDACs) regulate gene expression and protein activity crucial for cancer development. This review details how HDACs impact cancer by altering gene transcription and protein function.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cancer Biology

Background:

  • Histone deacetylases (HDACs) are critical regulators of gene expression.
  • HDACs influence chromatin structure by removing acetyl groups from histones.
  • Aberrant HDAC activity is implicated in cancer initiation and progression.

Purpose of the Study:

  • To comprehensively review the mechanisms by which HDACs regulate cancer-associated proteins.
  • To examine the impact of HDACs on gene transcription and protein function in cancer.
  • To elucidate the role of HDACs in tumorigenesis and cancer progression.

Main Methods:

  • Literature review of transcriptional and post-translational regulation by HDACs.
  • Analysis of HDAC targets beyond histones, including transcription factors and cellular proteins.

More Related Videos

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry
10:54

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry

Published on: November 21, 2025

An Acetyl-Click Chemistry Assay to Measure Histone Acetyltransferase 1 Acetylation
05:44

An Acetyl-Click Chemistry Assay to Measure Histone Acetyltransferase 1 Acetylation

Published on: January 26, 2024

Related Experiment Videos

Last Updated: Jul 13, 2026

Assays for Validating Histone Acetyltransferase Inhibitors
09:11

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry
10:54

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry

Published on: November 21, 2025

An Acetyl-Click Chemistry Assay to Measure Histone Acetyltransferase 1 Acetylation
05:44

An Acetyl-Click Chemistry Assay to Measure Histone Acetyltransferase 1 Acetylation

Published on: January 26, 2024

  • Examination of the functional consequences of HDAC activity in cancer models and human studies.

    • Main Results:

    • HDACs induce a non-permissive chromatin state, suppressing genes involved in tumorigenesis.
    • HDACs deacetylate non-histone proteins, affecting cell growth, differentiation, and apoptosis.
    • Altered HDAC activity significantly impacts multiple facets of cancer development.

    Conclusions:

    • HDACs play a multifaceted role in cancer through both transcriptional and post-translational modifications.
    • Understanding HDAC mechanisms provides insights into novel cancer therapeutic strategies.
    • Targeting HDACs represents a promising avenue for cancer treatment.