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,...
Inheritance of Chromatin Structures03:17

Inheritance of Chromatin Structures

Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying DNA...
Euchromatin01:01

Euchromatin

The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions take up more dye, appearing darker, while the less-compact areas take up less dye and appear lighter. Based on the compaction level, chromatins are classified into two primary forms – euchromatin and heterochromatin.
Euchromatin is the less dense region of the chromatin and stains lighter. Euchromatin contains histone H3 extensively...
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...
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...
Properties of Enantiomers and Optical Activity02:24

Properties of Enantiomers and Optical Activity

It is essential to understand the difference between chiral and achiral interactions and the implications thereof in optical activity and their applications. Just as our feet, which are chiral, interact uniquely with chiral objects, such as a pair of shoes, but identically with achiral socks, enantiomers of a molecule exhibit different properties only when they interact with other chiral media. An example of a significant implication from this facet is the phenomenon known as optical activity,...

You might also read

Related Articles

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

Sort by
Same author

PSAQ<sup>+1</sup>: Absolute Protein Quantification Using a <sup>13</sup>C<sub>1</sub>-Labeled Protein Standard, Coisolation of Peptide Pairs and LC-PRM.

Analytical chemistry·2026
Same author

Environmental and Genetic Perturbations of the Sperm Epigenome.

Advances in experimental medicine and biology·2026
Same author

Multiple Roles of Protamine Kinase SRPK1 and Phosphatase PP1γ in Sperm Development.

Proteomics·2026
Same author

Impact of Arsenite on Transient and Persistent Histone H3 Modifications and Transcriptional Response.

Chemical research in toxicology·2026
Same author

Uneven impacts: how male diet modulates the sperm epigenome and impacts embryo development and pregnancy health†.

Biology of reproduction·2025
Same author

Correction: Large-scale transcriptomic analyses reveal downstream target genes of ZFY1 and ZFY2 transcription factors in male germ cells.

Cell death and differentiation·2025

Related Experiment Video

Updated: Jun 14, 2026

Chromatin Immunoprecipitation (ChIP) using Drosophila tissue
13:47

Chromatin Immunoprecipitation (ChIP) using Drosophila tissue

Published on: March 23, 2012

Both L-Lactyl and D-Lactyl Enantiomers Modify Histones in Mouse Testis.

Julie Manessier1, Hassan Hijazi1, Lisa Vizzini1

  • 1University Grenoble Alpes, CEA, INSERM, UA13 BGE, CNRS, CEA, UAR 2048, Grenoble, France.

Molecular & Cellular Proteomics : MCP
|June 12, 2026
PubMed
Summary

Histone lactylation, a dynamic gene regulator, was identified in mouse testis, revealing both L- and D-lactylation enantiomers on histones H3 and H4. Surprisingly, balanced enantiomer levels were found despite L-lactate abundance, suggesting unique regulatory mechanisms.

Keywords:
D-lactylationL-lactylationacetylationhistoneslactatelactylationmethylglyoxalmouse testisracemic mixturetargeted proteomic analysis

More Related Videos

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
05:58

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells

Published on: February 24, 2026

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

Related Experiment Videos

Last Updated: Jun 14, 2026

Chromatin Immunoprecipitation (ChIP) using Drosophila tissue
13:47

Chromatin Immunoprecipitation (ChIP) using Drosophila tissue

Published on: March 23, 2012

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
05:58

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells

Published on: February 24, 2026

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

Area of Science:

  • Epigenetics and Molecular Biology
  • Proteomics
  • Reproductive Biology

Background:

  • Dynamic histone post-translational modifications orchestrate gene expression.
  • Histone lysine lactylation is a recently discovered modification with roles in pathology, but less understood in normal tissues.
  • Lactylation exists as L- and D-enantiomers, with L-lactate's abundance suggesting it might be the primary form.

Purpose of the Study:

  • To identify and quantify L- and D-lactylation on histones in normal mouse testis.
  • To investigate lactylation patterns in male germ cells.
  • To compare lactylation with acetylation on specific histone residues.

Main Methods:

  • Proteomic analysis to identify L- and D-lactylation on histones H3 and H4.
  • Development of targeted proteomic assays using synthetic lactylated peptides for accurate quantification.
  • Reversed-phase chromatography to separate lactylated histone peptides.
  • Analysis of histones from meiotic and post-meiotic male germ cells.

Main Results:

  • Both L- and D-lactylation were identified on histones H3 and H4 in mouse testis.
  • Abundance ratios of L- to D-lactylation ranged from 0.4 to 1.6 on seven residues, despite higher L-lactate levels.
  • Histone H3 residues 18 and 23 showed balanced amounts of both enantiomers in germ cells.
  • Lactylation stoichiometry was low (0.01-0.44%) but more abundant than acetylation on the C-terminal half of H3/H4.

Conclusions:

  • Mouse testis exhibits both L- and D-lactylation on histones H3 and H4.
  • The presence of balanced enantiomers suggests a complex regulatory mechanism for lactylation.
  • Lactylation may play a distinct role in gene regulation, particularly in male germ cells and on C-terminal histone regions.