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 Experiment Videos

Acetylated nucleosome assembly on telomeric DNAs.

Stefano Cacchione1, José Luis Rodríguez, Rosella Mechelli

  • 1Dipartimento di Genetica e Biologia Molecolare, Fondazione Istituto Pasteur-Fondazione Cenci Bolognetti, Università di Roma La Sapienza, Piazzale A. Moro 5, 00185, Roma, Italy.

Biophysical Chemistry
|July 25, 2003
PubMed
Summary

Histone acetylation enhances nucleosome formation and DNA accessibility across various sequences, including telomeres. Removing histone tails slightly destabilizes nucleosomes, with telomeres showing less impact, suggesting complex roles beyond simple electrostatic interactions.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Unraveling the phenolic profiles of Clinopodium bolivianum (Benth.) Kuntze and Minthostachys mollis (Benth.) Griseb.: A comprehensive LC-QtoF metabolomic study of underexplored Peruvian medicinal plants.

Journal of pharmaceutical and biomedical analysis·2026
Same author

Multiple sclerosis-associated EBNA2 variants influence the response to peginterferon beta-1a therapy.

Journal of autoimmunity·2026
Same author

Modulating TERRA G-quadruplexes with ligands: impact on telomeric DNA:RNA hybrids and ALT mechanisms.

Nucleic acids research·2025
Same author

Influence of oral and skin microbiota on multiple sclerosis risk and severity: A mendelian randomization analysis.

Multiple sclerosis and related disorders·2025
Same author

Clinical and Endoscopic-Histological Features of Multifocal and Corpus-Restricted Atrophic Gastritis Patients With Non-Cardia Gastric Cancer or Dysplasia: A Multicenter, Cross-Sectional Study.

Clinical and translational gastroenterology·2025
Same author

A disease-specific convergence of host and Epstein-Barr virus genetics in multiple sclerosis.

Proceedings of the National Academy of Sciences of the United States of America·2025

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Biochemistry

Background:

  • Nucleosomes are fundamental units of DNA packaging in eukaryotes.
  • Histone N-terminal domains play crucial roles in nucleosome structure and function.
  • Histone acetylation is a key epigenetic modification influencing chromatin accessibility.

Purpose of the Study:

  • To investigate the role of histone N-terminal domains in nucleosome stability.
  • To determine the impact of histone acetylation and tail removal on nucleosomes assembled on different DNA sequences, including telomeric DNA.

Main Methods:

  • Competitive reconstitution assays to study nucleosome formation.
  • Selective trypsinization to remove histone terminal domains.
  • Micrococcal nuclease kinetics to assess DNA accessibility.

Related Experiment Videos

Main Results:

  • Histone hyperacetylation favors nucleosome formation across all tested DNA sequences.
  • Removal of histone tails decreases nucleosome stability, with a lesser effect on telomeric sequences.
  • Acetylated nucleosomes exhibit enhanced DNA accessibility on both telomeric and average DNA sequences.

Conclusions:

  • Histone acetylation has a complex role in nucleosome stability and DNA accessibility, extending beyond electrostatic interactions.
  • Telomeric DNA sequences interact minimally with histone tails.
  • Histone N-terminal domains contribute to nucleosome stability, but their role is sequence-dependent.