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

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...
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...
Position-effect Variegation02:32

Position-effect Variegation

In 1928, a German botanist Emil Heitz observed the moss nuclei with a DNA binding dye. He observed that while some chromatin regions decondense and spread out in the interphase nucleus, others do not. He termed them euchromatin and heterochromatin, respectively. He proposed that the heterochromatin regions reflect a functionally inactive state of the genome. It was later confirmed that heterochromatin is transcriptionally repressed, and euchromatin is transcriptionally active chromatin.
Heterochromatin02:38

Heterochromatin

The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...

You might also read

Related Articles

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

Sort by
Same author

Disruption and nebulization of lipid vesicles using surface acoustic waves for direct mass spectrometry.

Lab on a chip·2025
Same author

Development of an Optimized Two-Step Solid-Phase Extraction Method for Urinary Nucleic Acid Adductomics.

Biomolecules·2025
Same author

Lyophilized Small Extracellular Vesicles (sEVs) Derived from Human Adipose Stem Cells Maintain Efficacy to Promote Healing in Neuronal Injuries.

Biomedicines·2025
Same author

Trace Analysis of C<sub>4</sub>F<sub>7</sub>N Insulating Gas Mixtures by Spontaneous Raman Spectroscopy and Gas Chromatography.

ACS omega·2024
Same author

Shake It Off! Acoustic Manipulation of Lipid Vesicles for Mass Spectrometric Analysis.

Analytical chemistry·2023
Same author

Comparing ELISA and LC-MS-MS: A Simple, Targeted Postmortem Blood Screen.

Journal of analytical toxicology·2021

Related Experiment Video

Updated: Jun 12, 2026

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

Time-of-flights and traps: from the Histone Code to Mars.

Robert J Cotter1, Stepehen Swatkoski, Luann Becker

  • 1Middle Atlantic Mass Spectrometry Laboratory, Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. rcotter@jhmi.edu

European Journal of Mass Spectrometry (Chichester, England)
|June 10, 2010
PubMed
Summary
This summary is machine-generated.

This paper explores two mass spectrometer designs: a tandem time-of-flight instrument for analyzing histone modifications and the Mars Organic Mass Analyzer (MOMA) for environmental and biological analysis.

More Related Videos

Exploring the Effects of Spaceflight on Mouse Physiology using the Open Access NASA GeneLab Platform
11:08

Exploring the Effects of Spaceflight on Mouse Physiology using the Open Access NASA GeneLab Platform

Published on: January 13, 2019

Low-Cost Automated Flight Intercept Trap for the Temporal Sub-Sampling of Flying Insects Attracted to Artificial Light at Night
06:19

Low-Cost Automated Flight Intercept Trap for the Temporal Sub-Sampling of Flying Insects Attracted to Artificial Light at Night

Published on: December 29, 2021

Related Experiment Videos

Last Updated: Jun 12, 2026

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

Exploring the Effects of Spaceflight on Mouse Physiology using the Open Access NASA GeneLab Platform
11:08

Exploring the Effects of Spaceflight on Mouse Physiology using the Open Access NASA GeneLab Platform

Published on: January 13, 2019

Low-Cost Automated Flight Intercept Trap for the Temporal Sub-Sampling of Flying Insects Attracted to Artificial Light at Night
06:19

Low-Cost Automated Flight Intercept Trap for the Temporal Sub-Sampling of Flying Insects Attracted to Artificial Light at Night

Published on: December 29, 2021

Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Instrument Development

Background:

  • Mass spectrometry is crucial for analyzing complex biological molecules.
  • Histone modifications play vital roles in gene regulation.
  • Developing advanced mass spectrometers is key for detailed biological insights.

Purpose of the Study:

  • To present two distinct mass spectrometer designs.
  • To showcase applications of a novel tandem time-of-flight mass spectrometer for histone analysis.
  • To introduce the Mars Organic Mass Analyzer (MOMA) prototype for broader applications.

Main Methods:

  • Utilized a curved-field reflectron tandem time-of-flight mass spectrometer.
  • Employed chemical derivatization for quantitative analysis of histone acetylation and deacetylation.
  • Developed a prototype low voltage, low power ion trap mass spectrometer (MOMA).

Main Results:

  • Demonstrated quantitative assessment of histone acetylation sites using deuteroacetylated analogs.
  • Identified sirtuin targets on histones via biotin replacement of deacetylated residues.
  • Presented MOMA as a viable prototype for future environmental, biological, and clinical analyses.

Conclusions:

  • The presented tandem time-of-flight mass spectrometer offers practical solutions for studying histone modifications.
  • MOMA represents a promising development in portable mass spectrometry for diverse analytical needs.
  • Advancements in mass spectrometer design continue to expand possibilities in biological and environmental research.