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

Cooperative DNA binding by lambda integration protein--a key component of specificity.

S J Minter, G M Clore, A M Gronenborn

    European Journal of Biochemistry
    |December 15, 1986
    PubMed
    Summary

    Bacteriophage lambda integration protein (Int) shows cooperative binding to DNA attachment sites. This cooperativity, essential for strong binding, involves interactions between Int molecules at adjacent DNA binding sites.

    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

    Integrated BioNMR - "getting by with a little help from my friends".

    Journal of magnetic resonance (San Diego, Calif. : 1997)·2019
    Same author

    Harnessing the Combined Power of SAXS and NMR.

    Advances in experimental medicine and biology·2019
    Same author

    Myristoylation as a general method for immobilization and alignment of soluble proteins for solid-state NMR structural studies.

    Journal of biomolecular NMR·2003
    Same author

    Structure and dynamics of MarA-DNA complexes: an NMR investigation.

    Journal of molecular biology·2001
    Same author

    Folded monomer of HIV-1 protease.

    The Journal of biological chemistry·2001
    Same author

    Probing the structure and stability of a hybrid protein: the human-E. coli thioredoxin chimera.

    Biochemistry·2001

    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Genetics

    Background:

    • The lambda integration protein (Int) mediates the integration of bacteriophage lambda DNA into the host genome.
    • Understanding Int-DNA interactions is crucial for comprehending viral DNA integration mechanisms.

    Purpose of the Study:

    • To quantitatively analyze the binding of lambda integration protein (Int) to specific DNA sequences.
    • To investigate the cooperative binding behavior of Int to the lambda attachment site (lambda attP).

    Main Methods:

    • Quantitative analysis of nitrocellulose filter binding data using the Clore, Gronenborn, and Davies method.
    • Modeling of Int binding to P' and P1 sites within the lambda attP region.

    Main Results:

    Related Experiment Videos

    • Lambda Int protein exhibits cooperative binding to specific recognition sites within the lambda attP region.
    • Optimal equilibrium constants were determined for P' (3.0 x 10^10 M^-1) and P1 (1.9 x 10^10 M^-1) sites.
    • A high cooperativity parameter (alpha = 172) was observed, indicating strong cooperative interactions.

    Conclusions:

    • Cooperative interaction between Int molecules at adjacent binding sites is essential for strong binding to lambda attP.
    • The presence of binding site arrays in lambda attP, unlike sequences with single sites, is critical for this cooperative binding.