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

Defined structural changes occur in a nucleosome upon Amt1 transcription factor binding.

Cindy L White1, Karolin Luger

  • 1Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO-80523-1870, USA.

Journal of Molecular Biology
|September 15, 2004
PubMed
Summary

Transcription factor Amt1 binds nucleosomes with high affinity, causing DNA end release from histones. This reveals nucleosomes can structurally adapt to external influences.

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

PARP1 Exhibits an Enzymatically Inactive Chromatin Binding Mode.

bioRxiv : the preprint server for biology·2026
Same author

Structure of the human HIRA histone chaperone with a nucleosome suggests a stepwise nucleosome assembly mechanism.

bioRxiv : the preprint server for biology·2026
Same author

TFAM organizes DNA into compact higher order structures.

bioRxiv : the preprint server for biology·2026
Same author

Histone diversity in the archaeal domain of life.

Nature communications·2026
Same author

The Expanding Histone Universe: Histone-Based DNA Organization in Noneukaryotic Organisms.

Annual review of biophysics·2025
Same author

Histone PARylation factor 1: a review of its role in the DNA damage response.

Nucleic acids research·2025

Area of Science:

  • Molecular biology
  • Structural biology
  • Biophysics

Background:

  • Nucleosomes are fundamental units of DNA packaging in eukaryotes.
  • Transcription factors regulate gene expression by binding to specific DNA sequences.
  • Understanding transcription factor-nucleosome interactions is crucial for gene regulation studies.

Purpose of the Study:

  • To investigate the binding of transcription factor Amt1 to nucleosomes.
  • To characterize the structural consequences of factor binding on nucleosome structure.
  • To explore the role of adjacent DNA sequences in facilitating factor binding.

Main Methods:

  • Fluorescence resonance energy transfer (FRET) to monitor DNA-histone interactions.
  • Biophysical techniques to quantify binding affinities.

Related Experiment Videos

  • Biochemical assays to assess histone subunit integrity.

    • Main Results:

    • The DNA binding domain of Amt1 binds nucleosomes with a threefold reduced affinity compared to free DNA.
    • Transcription factor binding induces partial dissociation of DNA ends from the histone octamer.
    • No dissociation or rearrangement of histone subunits was observed.
    • An adjacent poly(dA.dT) sequence facilitates but is not essential for factor binding.

    Conclusions:

    • Nucleosomes can undergo structural adaptation in response to transcription factor binding.
    • The binding of Amt1 to nucleosomes involves dynamic changes in DNA-histone interactions.
    • The study provides novel insights into the mechanisms of gene regulation at the chromatin level.