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

Nucleosome Remodeling02:54

Nucleosome Remodeling

11.2K
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...
11.2K
The Nucleosome02:33

The Nucleosome

18.9K
DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...
18.9K
The Nucleosome02:33

The Nucleosome

5.1K
5.1K
The Nucleosome01:19

The Nucleosome

4.1K
Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...
4.1K
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

14.5K
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...
14.5K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

2.4K
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...
2.4K

You might also read

Related Articles

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

Sort by
Same author

Comparative effectiveness of first-line targeted therapies in ALK-positive non-small cell lung cancer: real-world evidence of tyrosine kinase inhibitors.

Lung cancer (Amsterdam, Netherlands)·2026
Same author

Tandem bromodomains of BRD4 cooperatively read poly-acetylated nucleosomes to enhance chromatin engagement and regulate breast cancer phenotypes.

bioRxiv : the preprint server for biology·2026
Same author

Discovery of Small-Molecule Antagonists of PHF1 and 19 Demonstrates the Ligandability of PRC2 Accessory Proteins.

ACS bio & med chem Au·2026
Same author

Long-read analysis of tetrameric microsatellites with vmwhere supports GGAA repeat length-dependent chromatin state association in Ewing sarcoma.

bioRxiv : the preprint server for biology·2026
Same author

Rapid CRISPR-Cas9 Genome Editing in S. cerevisiae.

bioRxiv : the preprint server for biology·2026
Same author

A submission checklist to improve transparency and replicability of functional genomics data analyses.

The Journal of biological chemistry·2026
Same journal

Correction: Characterization of Mast2 kinase defines structural features, regulation, and substrates.

The Journal of biological chemistry·2026
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
Same journal

Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

The Journal of biological chemistry·2026
Same journal

Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

The Journal of biological chemistry·2026
Same journal

YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

The Journal of biological chemistry·2026
Same journal

ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

The Journal of biological chemistry·2026
See all related articles

Related Experiment Video

Updated: Feb 8, 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

23.1K

PBRM1 bromodomains variably influence nucleosome interactions and cellular function.

Mariesa J Slaughter1,2, Erin K Shanle3, Andrew W McFadden2

  • 1From the Department of Genetics, Curriculum in Genetics and Molecular Biology.

The Journal of Biological Chemistry
|July 11, 2018
PubMed
Summary
This summary is machine-generated.

Polybromo 1 (PBRM1) bromodomains BD2 and BD4 bind to histones, with neighboring domains modulating this interaction. Mutations in PBRM1

Keywords:
BAF180PBRM1bromodomaincancerchromatinchromatin regulationchromatin structurehistone acetylationhistone methylationhistone modificationhistones

More Related Videos

Detection of Post-translational Modifications on Native Intact Nucleosomes by ELISA
07:13

Detection of Post-translational Modifications on Native Intact Nucleosomes by ELISA

Published on: April 26, 2011

17.8K
Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques
05:58

Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques

Published on: September 6, 2024

1.6K

Related Experiment Videos

Last Updated: Feb 8, 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

23.1K
Detection of Post-translational Modifications on Native Intact Nucleosomes by ELISA
07:13

Detection of Post-translational Modifications on Native Intact Nucleosomes by ELISA

Published on: April 26, 2011

17.8K
Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques
05:58

Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques

Published on: September 6, 2024

1.6K

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cancer Research

Background:

  • Chromatin remodelers utilize bromodomains (BDs) for histone recognition.
  • Polybromo 1 (PBRM1), a component of the PBAF chromatin-remodeling complex, is frequently mutated in clear cell renal cell carcinoma (ccRCC).
  • Individual PBRM1 BD binding specificities have been explored, but the influence of neighboring BDs on nucleosome recognition remains unclear.

Purpose of the Study:

  • To investigate the histone-binding characteristics of individual and combined PBRM1 bromodomains.
  • To determine how neighboring bromodomains influence PBRM1's nucleosome interactions.
  • To analyze the impact of ccRCC-associated mutations in PBRM1 on chromatin interactions and ccRCC cell proliferation.

Main Methods:

  • Histone microarrays and intact nucleosome assays were employed to study PBRM1 BD binding.
  • Biochemical and mutational analyses were performed on full-length PBRM1 and its domains.
  • ccRCC cell proliferation assays were conducted to assess the functional impact of mutations.

Main Results:

  • PBRM1 BD2 and BD4 mediate binding to acetylated histone peptides and modified nucleosomes.
  • Neighboring BDs (BD1, BD5, BD3) variably modulate the nucleosome binding of BD2 and BD4.
  • ccRCC-associated missense mutations in PBRM1 BD4 disrupt chromatin interactions and accelerate ccRCC cell proliferation.

Conclusions:

  • PBRM1 BD4 is critical for proper PBRM1 function in chromatin regulation.
  • Mutations in PBRM1 BD4 enhance ccRCC cell growth, highlighting its oncogenic role.
  • PBRM1 BD4 mutations may represent a potential clinical target, given the link between PBRM1 and immune checkpoint inhibitor sensitivity.