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

Activity changes in lac repressor with cysteine oxidation.

S P Manly, K S Matthews

    The Journal of Biological Chemistry
    |May 10, 1979
    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

    The lactose repressor system: paradigms for regulation, allosteric behavior and protein folding.

    Cellular and molecular life sciences : CMLS·2006
    Same author

    Engineered disulfide linking the hinge regions within lactose repressor dimer increases operator affinity, decreases sequence selectivity, and alters allostery.

    Biochemistry·2001
    Same author

    Structure of a variant of lac repressor with increased thermostability and decreased affinity for operator.

    Journal of molecular biology·2001
    Same author

    p53 unfolding detected by CD but not by tryptophan fluorescence.

    Biochemical and biophysical research communications·2001
    Same author

    Ion concentration and temperature dependence of DNA binding: comparison of PurR and LacI repressor proteins.

    Biochemistry·2001
    Same author

    Protein-DNA binding correlates with structural thermostability for the full-length human p53 protein.

    Biochemistry·2001
    Same journal

    Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

    The Journal of biological chemistry·2026
    Same journal

    Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

    The Journal of biological chemistry·2026
    Same journal

    Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

    The Journal of biological chemistry·2026
    Same journal

    YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

    The Journal of biological chemistry·2026
    Same journal

    ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

    The Journal of biological chemistry·2026
    Same journal

    PAX8 controls proximal tubule epithelial identity and stress response through epigenetic modification of distal regulatory elements.

    The Journal of biological chemistry·2026
    See all related articles

    Prior modification of lac repressor protein

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Protein Chemistry

    Background:

    • Lac repressor protein controls the transcription of the lac operon.
    • N-bromosuccinimide (NBS) is a reagent used to study protein oxidation.
    • Understanding protein-DNA interactions is crucial for gene regulation.

    Purpose of the Study:

    • To investigate the impact of cysteine modification and nonspecific DNA on lac repressor's reaction with N-bromosuccinimide.
    • To determine how these factors affect operator DNA binding activity.
    • To identify key regions within the repressor protein involved in specific DNA binding.

    Main Methods:

    • Chemical modification of lac repressor protein using N-bromosuccinimide.
    • Assessing DNA binding activities (operator, inducer, nonspecific) after treatment.

    Related Experiment Videos

  • Analyzing the oxidation of cysteine and methionine residues.

    • Main Results:

    • N-bromosuccinimide oxidizes cysteine and methionine residues in lac repressor.
    • Oxidation leads to loss of operator DNA binding but retains inducer and nonspecific DNA binding.
    • Prior cysteine modification or presence of nonspecific DNA protects operator binding function.
    • Cysteine 107 and the core region are critical for specific operator binding.

    Conclusions:

    • Cysteine modification and nonspecific DNA binding influence lac repressor's susceptibility to N-bromosuccinimide.
    • The core region, particularly around cysteine 107, is vital for specific lac operator recognition.
    • Nonspecific DNA binding appears to protect the core region of the repressor protein.