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An E. coli gene product required for lambda site-specific recombination.

H I Miller, D I Friedman

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    |July 1, 1980
    PubMed
    Summary
    This summary is machine-generated.

    Mutations in the himA gene of E. coli impair site-specific recombination essential for bacteriophage lambda lysogeny. The himA protein likely facilitates DNA-protein interactions, impacting various phage integration and excision processes.

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    Area of Science:

    • Molecular Biology
    • Genetics
    • Microbiology

    Background:

    • Site-specific recombination is crucial for bacteriophage lambda lysogeny.
    • The himA gene's role in this process was previously unclear.
    • Understanding himA function is key to deciphering DNA recombination mechanisms.

    Purpose of the Study:

    • To characterize himA mutations in E. coli.
    • To elucidate the function of the himA gene product in site-specific recombination.
    • To investigate the pleiotropic effects of himA mutations.

    Main Methods:

    • Selection of E. coli himA mutants unable to support lambda site-specific recombination.
    • Genetic mapping of himA mutations.
    • Complementation tests and dominance studies.
    • Analysis of himA mutation effects on various phage integration and excision events.

    Main Results:

    • Three noncomplementing himA mutations were identified, with one being a nonsense mutation, confirming a protein product.
    • himA mutations significantly reduced both integrative and excisive site-specific recombination for bacteriophage lambda.
    • himA mutations displayed pleiotropic effects, impacting integration of other phages, phage mu growth, and precise excision of phage mu and Tn elements.

    Conclusions:

    • The himA protein is likely essential for or regulates site-specific recombination.
    • The pleiotropic nature of himA mutations suggests a general role in facilitating protein-DNA interactions.
    • himA protein may act as an auxiliary factor in diverse DNA manipulation processes.