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RNA polymerase interaction with dnaB protein and lambda P protein during lambda replication.

M D McKinney, J A Wechsler

    Journal of Virology
    |November 1, 1983
    PubMed
    Summary

    Mutations in rpoB altered the Escherichia coli GroP- phenotype, affecting lambda bacteriophage plating. This suggests RNA polymerase, dnaB, and lambda P proteins form a complex essential for lambda replication.

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    Growth of phages lambda and phiX174 under Plban protein control in the absence of host dnaB function.

    Virology·1981

    Area of Science:

    • Microbiology
    • Molecular Biology
    • Genetics

    Background:

    • The Escherichia coli GroP- phenotype is characterized by a reduced ability to plate lambda bacteriophage.
    • This phenotype is often associated with specific mutations in the dnaB gene.

    Purpose of the Study:

    • To investigate the role of rpoB mutations in the Escherichia coli GroP- phenotype.
    • To elucidate the functional interactions between dnaB, rpoB, and lambda P proteins in bacteriophage lambda replication.

    Main Methods:

    • Genetic analysis of Escherichia coli mutants.
    • Phenotypic characterization of bacteriophage lambda plating efficiency.
    • Allele specificity analysis of rpoB, dnaB, and lambda P mutations.

    Main Results:

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    • Certain rpoB mutations were found to modify the GroP- phenotype.
    • The observed effects of rpoB mutations were dependent on the specific alleles involved.
    • Both dnaB and lambda P alleles demonstrated allele-specific participation in the GroP- phenotype.

    Conclusions:

    • RNA polymerase (encoded by rpoB), dnaB protein, and lambda P protein interact functionally.
    • This functional complex is crucial for the replication of bacteriophage lambda.