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

Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor.

K Kwon1, E D Streaker, S Ruparelia

  • 1Department of Chemistry and Biochemistry, University of Maryland, MD 20742, USA.

Journal of Molecular Biology
|December 22, 2000
PubMed
Summary

Escherichia coli biotin repressor dimerization is essential for DNA binding. Mutational analysis reveals disordered surface loops in the corepressor-binding domain are critical for this self-assembly and DNA interaction.

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

Development of Monoclonal Antibodies for Identifying Plant-Parasitic Nematodes.

Journal of nematology·2025
Same author

Oral health students' perceptions of the learning environment in Australia and New Zealand: A DREEM study.

European journal of dental education : official journal of the Association for Dental Education in Europe·2024
Same author

Demirjian method and Willems method to study the dental age of adolescents in Shanghai before and after 10 years.

Folia morphologica·2022
Same author

Spontaneous Formation of Star-Shaped Surface Patterns in a Driven Bose-Einstein Condensate.

Physical review letters·2021
Same author

Age estimation for children and young adults by volumetric analysis of upper anterior teeth using cone-beam computed tomography data.

Folia morphologica·2020
Same author

Chlorhexidine sensitivity in staphylococci isolated from patients with central line-associated bloodstream infection.

The Journal of hospital infection·2019

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • The Escherichia coli biotin repressor (BirA) regulates biotin operon expression.
  • BirA's DNA binding is allosterically activated by the corepressor bio-5'-AMP, which induces repressor dimerization.
  • The structural basis for BirA dimerization remains unclear due to the lack of a high-resolution structure of the dimer.

Purpose of the Study:

  • To investigate the role of the corepressor-binding domain in BirA dimerization and DNA binding.
  • To identify the structural elements involved in BirA self-assembly and corepressor-induced dimerization.

Main Methods:

  • Site-directed mutagenesis of five residues within the BirA corepressor-binding domain.
  • Analysis of mutant protein DNA-binding affinity.

Related Experiment Videos

  • Assessment of mutant protein self-assembly (dimerization) properties.
  • Mapping of mutations onto the three-dimensional structure of the apo-repressor.

    • Main Results:

    • Four out of five mutants showed defects in DNA binding.
    • These DNA-binding deficient mutants also exhibited compromised self-assembly.
    • Mutations were located in partially disordered surface loops, one known to interact with the corepressor.
    • These loops are suggested to be involved in corepressor-induced dimerization.

    Conclusions:

    • Multiple disordered surface loops within the corepressor-binding domain are crucial for BirA dimerization.
    • Corepressor-induced dimerization, mediated by these loops, is essential for sequence-specific DNA binding by the biotin repressor.
    • These findings provide insights into the allosteric regulation mechanism of BirA.