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Related Experiment Videos

Escherichia coli recA gene product inactivates phage lambda repressor.

J W Roberts, C W Roberts, N L Craig

    Proceedings of the National Academy of Sciences of the United States of America
    |October 1, 1978
    PubMed
    Summary

    Escherichia coli recA protein inactivates phage lambda repressor by cleaving it into two fragments, mimicking in vivo SOS induction. This suggests recA protein possesses inherent proteolytic activity.

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    Area of Science:

    • Molecular Biology
    • Bacteriology
    • Virology

    Background:

    • Phage lambda repressor regulates viral gene expression.
    • SOS response is a DNA damage repair mechanism in E. coli.
    • RecA protein is central to SOS induction and recombination.

    Purpose of the Study:

    • To investigate the in vitro mechanism of phage lambda repressor inactivation.
    • To determine if purified recA protein can directly cleave lambda repressor.
    • To explore the proteolytic capabilities of recA protein.

    Main Methods:

    • In vitro incubation of purified Escherichia coli recA protein with purified phage lambda repressor.
    • ATP-dependent reaction assay.
    • Analysis of repressor cleavage products.

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    Main Results:

    • Purified recA protein cleaved phage lambda repressor into two fragments.
    • This cleavage reaction required ATP.
    • The in vitro reaction mirrored in vivo recA-dependent repressor inactivation during SOS induction.

    Conclusions:

    • RecA protein possesses direct proteolytic activity against phage lambda repressor.
    • This proteolytic activity is ATP-dependent.
    • The findings suggest recA protein's proteolytic function may be fundamental to its cellular roles.