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Gyrase . DNA complexes visualized as looped structures by electron microscopy.

C L Moore, L Klevan, J C Wang

    The Journal of Biological Chemistry
    |April 10, 1983
    PubMed
    Summary
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    Bacterial gyrase, an enzyme crucial for DNA replication, binds DNA to form loops. This enzyme likely has multiple DNA-binding sites, enabling it to constrain DNA during its function.

    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Microbial Genetics

    Background:

    • DNA gyrase is essential for bacterial DNA replication and topology.
    • Understanding gyrase's interaction with DNA is key to deciphering its mechanism.
    • Previous studies suggested gyrase's role in DNA supercoiling.

    Purpose of the Study:

    • To visualize and characterize the DNA-gyrase complex using electron microscopy.
    • To investigate the role of ATP in gyrase binding to DNA.
    • To elucidate the structural basis of gyrase's DNA-binding and supercoiling activity.

    Main Methods:

    • Electron microscopy was used to observe DNA-gyrase complexes.
    • Experiments involved linear and circular DNA substrates.
    • Non-hydrolyzable ATP analogs were employed to study ATP's role.

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    Main Results:

    • Gyrase forms nearly spherical particles at DNA intersections, creating looped structures.
    • ATP binding reduces the frequency of gyrase at DNA intersections.
    • Intermediate forms show gyrase at the base of supercoiled and relaxed DNA loops.

    Conclusions:

    • Gyrase possesses multiple DNA-binding sites, enabling it to hold DNA in constrained loops.
    • These structural observations provide insights into the mechanism of DNA supercoiling by gyrase.
    • The enzyme's ability to form and manipulate DNA loops is central to its function.