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 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,...
Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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.

You might also read

Related Articles

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

Sort by
Same author

Linker histones consolidate heterogenous nucleosome fiber contacts by linking together multiple nucleosomes.

Nature communications·2026
Same author

The solid and liquid states of chromatin.

Epigenetics & chromatin·2021
Same author

Condensed Chromatin Behaves like a Solid on the Mesoscale In Vitro and in Living Cells.

Cell·2020
Same author

Silencing the genome with linker histones.

Proceedings of the National Academy of Sciences of the United States of America·2020
Same author

Fluid-like chromatin: Toward understanding the real chromatin organization present in the cell.

Current opinion in cell biology·2020
Same author

Post-translational modifications and chromatin dynamics.

Essays in biochemistry·2019

Related Experiment Video

Updated: May 24, 2026

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
10:40

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

Dynamic fuzziness during linker histone action.

Steven J McBryant1, Jeffrey C Hansen

  • 1Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado, USA.

Advances in Experimental Medicine and Biology
|March 9, 2012
PubMed
Summary
This summary is machine-generated.

Linker histones, crucial for chromatin structure, utilize their intrinsically disordered C-terminal domain (CTD). This domain

More Related Videos

Expression Analysis of Mammalian Linker-histone Subtypes
14:40

Expression Analysis of Mammalian Linker-histone Subtypes

Published on: March 19, 2012

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
06:32

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Published on: March 9, 2022

Related Experiment Videos

Last Updated: May 24, 2026

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
10:40

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

Expression Analysis of Mammalian Linker-histone Subtypes
14:40

Expression Analysis of Mammalian Linker-histone Subtypes

Published on: March 19, 2012

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
06:32

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Published on: March 9, 2022

Area of Science:

  • Molecular Biology
  • Chromatin Biology
  • Structural Biology

Background:

  • Linker histones are essential for organizing chromatin structure.
  • They stabilize higher-order chromatin through nucleosome binding and protein interactions.

Purpose of the Study:

  • To highlight the structural and functional characteristics of the linker histone C-terminal domain (CTD).
  • To explore the role of intrinsic disorder and dynamic fuzziness in CTD function.

Main Methods:

  • Focus on structural and functional properties of the linker histone CTD.
  • Analysis of intrinsic disorder and interaction-induced secondary structure.
  • Investigation of dynamic fuzziness.

Main Results:

  • The linker histone CTD exhibits intrinsic disorder.
  • It undergoes secondary structure formation upon interaction.
  • Dynamic fuzziness is a key characteristic of the CTD.

Conclusions:

  • The inherent dynamic fuzziness of the CTD is a critical molecular mechanism.
  • This fuzziness underlies the essential functions of linker histones within the nucleus.