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Related Experiment Videos

lac repressor changes conformation upon binding to poly[dA-T)].

D E Kelsey, T C Rounds, S S York

    Proceedings of the National Academy of Sciences of the United States of America
    |June 1, 1979
    PubMed
    Summary
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    Escherichia coli lac repressor undergoes conformational changes upon binding to DNA. These structural shifts, identified using fluorescent labeling, likely enhance repressor-DNA interactions.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Genetics

    Background:

    • Escherichia coli lac repressor is a key transcriptional regulator.
    • Understanding repressor-DNA interactions is crucial for gene regulation studies.

    Purpose of the Study:

    • To investigate the conformational changes of E. coli lac repressor during DNA binding.
    • To characterize the dynamics of repressor-DNA association.

    Main Methods:

    • Selective fluorescent labeling of cysteine-140 on the lac repressor using N-(Iodoacetylaminoethyl)-1-naphthylamine-5-sulfonate.
    • Monitoring fluorescence intensity changes upon repressor binding to poly[d(A-T)].
    • Utilizing stopped-flow spectroscopy to analyze binding kinetics and conformational changes.

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    Main Results:

    • Fluorescent labeling of E. coli lac repressor at cysteine-140.
    • A 20% decrease in fluorescence intensity observed when labeled repressor binds to poly[d(A-T)].
    • Identification of at least two conformational changes with distinct half-lives (5.0 +/- 1.2 msec and 3.5 +/- 1.0 sec) during DNA binding.

    Conclusions:

    • The binding of E. coli lac repressor to DNA involves significant conformational rearrangements.
    • These conformational changes are likely essential for stabilizing the repressor-DNA complex.
    • The study provides insights into the dynamic nature of transcriptional regulation at the molecular level.