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

18.0K
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...
18.0K
Histone Modification02:32

Histone Modification

5.0K
5.0K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

10.1K
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...
10.1K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

10.0K
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....
10.0K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

2.8K
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...
2.8K
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

15.5K
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...
15.5K

You might also read

Related Articles

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

Sort by
Same author

Myeloid cell-mediated killing of B-ALL by CD38 and CD20 IgA antibody variants is enhanced by CD47/SIRPα interference.

Blood neoplasia·2026
Same author

Exploring the biochemical and biological functions of copper radical oxidases in the vascular wilt phytopathogen <i>Verticillium dahliae</i>.

Applied and environmental microbiology·2026
Same author

Blm10/PA200-Activated 20S Proteasomes Promote α-Synuclein Degradation and Bypass Proteasome Inhibition in Parkinson's Disease Models.

Aging cell·2026
Same author

EneA of Aspergillus fumigatus is a regulator of secondary metabolism and enhances nscA expression in presence of polyenes and Streptomyces.

Scientific reports·2026
Same author

The adapt-to-nutrient NRPS-like secondary metabolite gene cluster facilitates Verticillium dahliae adaptation to different nutrient environments.

PLoS genetics·2026
Same author

The <i>Aspergillus nidulans</i> transcription factor SclB governs the transition from vegetative to asexual development.

mBio·2026
Same journal

Lipid Metabolic Labeling to Study Site- and Lipid-Specific Long-Chain <i>S</i>-Acylation Dynamics.

ACS chemical biology·2026
Same journal

Inositol Thiophosphates as Inhibitors of Mammalian, Plant, and Fungal Phytases.

ACS chemical biology·2026
Same journal

Synthesis and Characterization of the Spectroscopic and Imaging Utilities of Two Indole-Based Cyan Fluorescent Nucleoside Analogues.

ACS chemical biology·2026
Same journal

Indole Ring Expansion and Rearrangement-Enabled Quinoline Scaffold Formation in the Biosynthesis of the Antitumor Monoterpene Indole Alkaloid Camptothecin.

ACS chemical biology·2026
Same journal

Intracellular Delivery of Peptides and Proteins with an Engineered Membrane Translocation Domain.

ACS chemical biology·2026
Same journal

Development of Next-Generation Fluoroacetamidine-Containing Activity-Based Probes for the Selective Labeling of the Protein Arginine Deiminases (PADs).

ACS chemical biology·2026
See all related articles

Related Experiment Video

Updated: Apr 18, 2026

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
10:09

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Published on: January 26, 2018

8.0K

Genetically encoding lysine modifications on histone H4.

Bryan J Wilkins1, Liljan E Hahn1, Svenja Heitmüller1

  • 1†Free Floater (Junior) Research Group "Applied Synthetic Biology", Institute for Microbiology and Genetics, Georg-August University Göttingen, Justus-von-Liebig Weg 11, 37077 Göttingen, Germany.

ACS Chemical Biology
|January 16, 2015
PubMed
Summary
This summary is machine-generated.

Researchers developed a new method to produce homogeneous histone H4 with various lysine modifications, enabling analysis of their impact on chromatin structure and antibody recognition.

More Related Videos

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

4.5K
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

4.7K

Related Experiment Videos

Last Updated: Apr 18, 2026

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
10:09

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Published on: January 26, 2018

8.0K
Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

4.5K
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

4.7K

Area of Science:

  • Biochemistry and Molecular Biology
  • Epigenetics and Chromatin Biology
  • Synthetic Biology

Background:

  • Post-translational modifications (PTMs) regulate protein function, necessitating methods for homogeneous production of modified proteins.
  • Genetic code expansion offers a versatile approach to produce modified proteins, bypassing limitations of natural enzymatic pathways.
  • Recombinant histone H4 production with specific PTMs has been challenging, hindering functional studies.

Discussion:

  • A novel strategy enables the production of homogeneous histone H4 with diverse lysine acylations, including acetylation, propionylation, butyrylation, and crotonylation.
  • This method allows for the incorporation of up to four simultaneous acetylations on histone H4, facilitating studies on chromatin array compaction.
  • The study investigates antibody discrimination between different lysine acylations using engineered histone H4.

Key Insights:

  • Direct genetic encoding of multiple lysine acylations on histone H4 is achieved.
  • The impact of simultaneous histone H4 acetylations on chromatin compaction is quantitatively analyzed.
  • Antibody specificity for distinct lysine acylations on histone H4 is evaluated.

Outlook:

  • This platform can be extended to produce histone variants with complex PTM patterns for comprehensive epigenomic studies.
  • Further research can explore the functional consequences of combinatorial lysine acylations in various biological contexts.
  • The developed methodology holds promise for advancing the understanding of epigenetic regulation and developing targeted therapeutics.