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

Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer

T Ellenberger1, D Fass, M Arnaud

  • 1Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts.

Genes & Development
|April 15, 1994
PubMed
Summary

The crystal structure of the E47 basic region helix-loop-helix (bHLH) transcription factor bound to DNA reveals its unique four-helix bundle. This structure clarifies how E47 interacts with DNA, impacting cell differentiation.

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

Safety of propofol use for general anaesthesia in Brugada syndrome patients: a 15-year experience.

Europace : European pacing, arrhythmias, and cardiac electrophysiology : journal of the working groups on cardiac pacing, arrhythmias, and cardiac cellular electrophysiology of the European Society of Cardiology·2025
Same author

Self-injection of a solution intended for topical use containing hyaluronic acid and vitamin B5.

Clinical and experimental dermatology·2020
Same author

An experimental comparison of two methods for warming intravenous crystalloid solutions.

Anaesthesia·2019
Same author

Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325° to 333deg.

Molecular microbiology·2017
Same author

[Combined approach for parotid lithiases: A 9 cases retrospective study].

Journal of stomatology, oral and maxillofacial surgery·2017
Same author

[Temporomandibular joint arthropathy in situ steroid injection].

Revue de stomatologie, de chirurgie maxillo-faciale et de chirurgie orale·2016

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Basic region helix-loop-helix (bHLH) proteins are crucial transcription factors regulating cell growth and differentiation.
  • These proteins form dimers, influencing DNA binding and transcriptional activity essential for tissue development.
  • Previous understanding of bHLH function was limited by a lack of detailed structural information.

Purpose of the Study:

  • To determine the crystal structure of the E47 bHLH domain in complex with DNA.
  • To elucidate the structural basis for DNA binding and sequence recognition by E47.
  • To compare the structural features of E47 bHLH with other related transcription factors.

Main Methods:

  • X-ray crystallography was employed to obtain the high-resolution structure of the E47 bHLH domain bound to DNA.

Related Experiment Videos

  • Structural analysis focused on the dimer interface, DNA-binding surface, and helix bundle organization.
  • Comparison with known structures, such as the bHLH-zipper protein Max, was performed.

    • Main Results:

    • The crystal structure reveals the E47 bHLH domain forms a parallel, four-helix bundle.
    • Distinct structural features differentiate the E47 bHLH from the bHLH-zipper protein Max.
    • The E47 dimer exhibits nonequivalent interactions with the two halves of the -CACCTG- DNA binding site.
    • Sequence discrimination at the E box may involve interactions with both DNA bases and the phosphodiester backbone.

    Conclusions:

    • The determined structure provides critical insights into the molecular mechanisms of E47-mediated gene regulation.
    • Structural differences explain the distinct DNA-binding activities of E47 compared to other bHLH proteins.
    • This work advances the understanding of how transcription factors recognize specific DNA sequences to control cellular processes.