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

Size and Structure of Viral Genomes01:26

Size and Structure of Viral Genomes

Viral genomes exhibit remarkable diversity in size, structure, and composition, influencing their replication strategies and interactions with host cells. These genomes consist of either DNA or RNA and may be linear or circular. Additionally, they can be single-stranded or double-stranded, with each configuration affecting how the virus propagates within a host. RNA viruses, for instance, generally have smaller genomes than DNA viruses, a factor that contributes to their high mutation rates and...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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...
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...
Nucleoid01:24

Nucleoid

The nucleoid represents a structurally and functionally distinct region within prokaryotic cells, where the cell's DNA and associated proteins are housed. Unlike eukaryotic cells, prokaryotes lack a membrane-bound nucleus, and the nucleoid facilitates the organization and accessibility of the genetic material within this constraint. The DNA in most bacteria and archaea exists as a single, circular, double-stranded molecule that is highly compacted through supercoiling and interactions with...

You might also read

Related Articles

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

Sort by
Same author

Taperin bundles F-actin at stereocilia pivot points enabling optimal lifelong mechanosensitivity.

The Journal of cell biology·2025
Same author

Structure of blood cell-specific tubulin and demonstration of dimer spacing compaction in a single protofilament.

The Journal of biological chemistry·2024
Same author

Determining structures of RNA conformers using AFM and deep neural networks.

Nature·2024
Same author

Encapsulated Ferritin-like Proteins: A Structural Perspective.

Biomolecules·2024
Same author

<i>Myxococcus xanthus</i> encapsulin cargo protein EncD is a flavin-binding protein with ferric reductase activity.

Proceedings of the National Academy of Sciences of the United States of America·2024
Same author

Structural basis of microtubule depolymerization by the kinesin-like activity of HIV-1 Rev.

Structure (London, England : 1993)·2023

Related Experiment Video

Updated: May 10, 2026

Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry
09:38

Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry

Published on: June 26, 2019

Structural basis for HIV-1 Rev recognition by the histone chaperone human Nap1.

Elif Eren1, Norman R Watts1, Dennis C Winkler2

  • 1Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA.

The Journal of Biological Chemistry
|May 8, 2026
PubMed
Summary

Human Nap1 (hNap1), a histone chaperone, stabilizes HIV-1 Rev protein structure. This interaction is key for viral RNA export and replication, offering new insights into HIV-1 dynamics.

Keywords:
HIV-1 RevRNA transportRNA-binding proteinRev response elementhistone chaperonenuclear transportnucleosomenucleosome assembly protein 1

More Related Videos

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors
08:33

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors

Published on: January 19, 2015

Detection of Viral RNA by Fluorescence in situ Hybridization (FISH)
10:16

Detection of Viral RNA by Fluorescence in situ Hybridization (FISH)

Published on: May 5, 2012

Related Experiment Videos

Last Updated: May 10, 2026

Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry
09:38

Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry

Published on: June 26, 2019

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors
08:33

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors

Published on: January 19, 2015

Detection of Viral RNA by Fluorescence in situ Hybridization (FISH)
10:16

Detection of Viral RNA by Fluorescence in situ Hybridization (FISH)

Published on: May 5, 2012

Area of Science:

  • Structural biology
  • Virology
  • Molecular biology

Background:

  • Human Nap1 (hNap1) is a histone chaperone crucial for chromatin dynamics.
  • The HIV-1 regulatory protein Rev is essential for nuclear export of viral RNA.
  • The interaction between hNap1 and Rev is functionally significant but structurally uncharacterized.

Purpose of the Study:

  • To elucidate the structural basis of the hNap1-Rev interaction.
  • To understand how hNap1 modulates Rev assembly and function.
  • To provide molecular insights into HIV-1 replication mechanisms.

Main Methods:

  • X-ray crystallography to determine hNap1 structure.
  • Cryo-electron microscopy to resolve the hNap1-Rev complex structure.
  • Surface plasmon resonance to quantify binding affinity.

Main Results:

  • The structure reveals hNap1 binds Rev dimers via its acidic concave surface.
  • hNap1 stabilizes Rev into a dimer-of-dimers tetramer, preventing aggregation.
  • This interaction enhances Rev's binding to the Rev Response Element and confirms low-micromolar affinity.

Conclusions:

  • hNap1 acts as a chaperone for Rev, modulating its assembly and function.
  • The hNap1-Rev interaction facilitates productive engagement with viral RNA.
  • This priming mechanism is crucial for efficient HIV-1 replication.