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

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...
The Nucleosome Core Particle02:10

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.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
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,...
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...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.

You might also read

Related Articles

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

Sort by
Same author

Individualized Biochemical Profiling in Drug Design: Integrating MultiOmics, Nanotechnology, and Machine Learning.

Current pharmaceutical biotechnology·2026
Same author

Current status and future perspectives on the mechanistic and pathophysiological understanding of long COVID.

Communications medicine·2026
Same author

Potential Involvement of Fructosylated Human Insulin and Serological Evidence in Subclinical Autoimmune Activity in Type 2 Diabetes Mellitus.

Current diabetes reviews·2026
Same author

Peroxynitrite-induced structural alterations render human fibrinogen more immunogenic: A possible mechanism of auto-immune response that acts as a proatherogenic marker.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy·2025
Same author

Leveraging RAS-mSIN1 interaction to selectively inhibit mTORC2 employing competitive RAS binding peptide: implications in breast cancer metastasis.

Oncogene·2025
Same author

Correction: Long COVID clinical evaluation, research and impact on society: a global expert consensus.

Annals of clinical microbiology and antimicrobials·2025

Related Experiment Video

Updated: Jun 19, 2026

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
09:26

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

Published on: March 26, 2017

Physicochemical studies on peroxynitrite-modified H3 histone.

Kiran Dixit1, M Asad Khan, Y D Sharma

  • 1Department of Biochemistry, Faculty of Medicine, Aligarh Muslim University (A.M.U.), Aligarh 202 002, Uttar Pradesh, India.

International Journal of Biological Macromolecules
|November 3, 2009
PubMed
Summary

Histones protect DNA but change structure under nitrosative stress. Peroxynitrite exposure caused calf thymus H3 histone to partially fold, protecting DNA from damage.

More Related Videos

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
07:20

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis

Published on: October 18, 2024

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry
05:52

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry

Published on: January 12, 2024

Related Experiment Videos

Last Updated: Jun 19, 2026

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
09:26

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

Published on: March 26, 2017

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
07:20

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis

Published on: October 18, 2024

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry
05:52

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry

Published on: January 12, 2024

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Histones are crucial for DNA packaging and protection within the cell nucleus.
  • Nitrosative stress, involving agents like peroxynitrite, can alter protein structure and function.
  • The structural response of histones to peroxynitrite is not fully understood.

Purpose of the Study:

  • To investigate the structural modifications of calf thymus H3 histone upon exposure to peroxynitrite.
  • To understand how H3 histone's structure changes under nitrosative stress conditions.

Main Methods:

  • UV spectroscopy
  • Fluorescence spectroscopy
  • Circular dichroism (CD) spectroscopy
  • Fourier-transform infrared (FTIR) spectroscopy
  • Polyacrylamide gel electrophoresis (PAGE)

Main Results:

  • Peroxynitrite-mediated oxidation and nitration induced a partially folded structure in H3 histone.
  • Native H3 histone exhibits an intrinsically disordered structure.
  • Spectroscopic analyses revealed significant structural alterations in modified H3 histone.

Conclusions:

  • H3 histone is highly sensitive to peroxynitrite, a reactive nitrogen species.
  • Under nitrosative stress, H3 histone can adopt altered structures.
  • These structural changes may serve a protective role for DNA against peroxynitrite-induced damage.