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Interactions between phage lambda replication proteins, lambda DNA and minicell membrane.

M Zylicz, K Taylor

    European Journal of Biochemistry
    |January 1, 1981
    PubMed
    Summary
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    Gentle lysis and fractionation of minicells revealed that phage lambda DNA and replication proteins associate with membranes. Detergents disrupt these interactions, affecting DNA-protein binding and membrane association.

    Area of Science:

    • Molecular Biology
    • Virology
    • Biochemistry

    Background:

    • Bacteriophage lambda DNA replication initiation involves specific proteins.
    • Minicells, lacking chromosomal DNA, are useful for studying plasmid replication and phage gene expression.
    • Prereplicative DNA intermediates can be trapped and analyzed.

    Purpose of the Study:

    • To develop gentle methods for minicell lysis and lysate fractionation.
    • To investigate the localization and binding of phage lambda DNA and replication proteins within infected minicells.
    • To determine the effects of ionic strength and detergents on these interactions.

    Main Methods:

    • Gentle lysis of minicells using T4 lysozyme without detergents.
    • Fractionation of lysates by equilibrium sedimentation in metrizamide density gradients.

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  • Analysis of DNA and protein distribution in membrane-bound and free fractions.

    • Main Results:

    • Phage lambda DNA, in prereplicative complexes, existed as membrane-bound and free forms.
    • Covalently-closed-circular lambda DNA was exclusively membrane-bound.
    • Lambda replication proteins (O and P) were primarily membrane-associated or bound to free DNA, not free proteins.
    • Triton X-100 displaced DNA from membranes and bound replication proteins to free DNA.
    • Sarcosyl disrupted the O protein-DNA complex.

    Conclusions:

    • Phage lambda DNA replication initiation involves membrane association.
    • Replication proteins O and P interact with both membranes and DNA.
    • Detergents differentially affect DNA-membrane and DNA-protein interactions during replication.