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

A histone octamer-like structure within TFIID

A Hoffmann1, C M Chiang, T Oelgeschläger

  • 1Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York 10021, USA.

Nature
|March 28, 1996
PubMed
Summary
This summary is machine-generated.

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

Mediator release assays based on human or murine immunoglobulin E in allergen standardization.

Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology·2007
Same author

[Retained foreign bodies from the surgical point of view].

Der Chirurg; Zeitschrift fur alle Gebiete der operativen Medizen·2006
Same author

Bulk chemical shifts in hydrogen-bonded systems from first-principles calculations and solid-state-NMR.

The journal of physical chemistry. B·2006
Same author

Transcriptional regulation via the NF-kappaB signaling module.

Oncogene·2006
Same author

Fast variability of tera-electron volt gamma rays from the radio galaxy M87.

Science (New York, N.Y.)·2006
Same author

Comment on "Photoemission study of YBa(2)Cu(3)O(y) thin films under light illumination".

Physical review letters·2006
Same journal

Daily briefing: 'Cyborg' cockroaches breathe underwater with printed suit.

Nature·2026
Same journal

China boosts prestigious grants for young scientists - will it ease competition?

Nature·2026
Same journal

Incoming US science academy chief vows to 'double down' on research.

Nature·2026
Same journal

Author Correction: Synthesis of enantioenriched atropisomers by biocatalytic deracemization.

Nature·2026
Same journal

Electrodeposited self-assembled molecules for perovskite photovoltaics.

Nature·2026
Same journal

Neutrino's nursery found: the 'Shadow Blaster'.

Nature·2026
See all related articles

The general transcription factor TFIID, crucial for gene activation, contains subunits with histone-like structures. This suggests a histone octamer-like complex within TFIID, offering new insights into transcription regulation.

Area of Science:

  • Molecular Biology
  • Gene Transcription
  • Chromatin Structure

Background:

  • The general transcription factor TFIID initiates gene transcription by binding to core promoters.
  • TFIID mediates the effects of transcriptional activators, but its structural organization remains unclear.
  • Previous studies identified TBP and TAFs within TFIID, with limited understanding of their structural roles.

Purpose of the Study:

  • To investigate the structural organization of the human TFIID complex.
  • To explore the potential histone-like structural relevance of TFIID subunits.
  • To elucidate the mechanism of transcriptional activation mediated by TFIID.

Main Methods:

  • Biochemical analyses of human TFIID subunits (hTAF80, hTAF31, hTAF20/15).

Related Experiment Videos

  • Examination of native TFIID complexes.
  • Crystallographic studies of TFIID components.

    • Main Results:

    • Biochemical evidence supports structural relevance of histone homologies in hTAF80, hTAF31, and hTAF20/15.
    • Analysis of native TFIID complexes revealed a histone octamer-like TAF complex.
    • Crystallographic data further supports the proposed structural model.

    Conclusions:

    • Human TFIID contains subunits with significant histone homologies.
    • A histone octamer-like TAF complex exists within TFIID.
    • This structural finding provides new insights into TFIID function and transcriptional activation.