Summary
Effect of temperature-sensitive, assembly-defective mutations in Escherichia coli RNA polymerase β (rpoB) or β′ subunit gene (rpoC) was investigated on the expression of wild-type rpoB +C+operon, which was introduced by infection of a lambda transducing phage λdrif + (rpoB +)-6 after UV-irradiation of the mutant cells. In rpoB2·rpoB7 strain which accumulates assembly-intermediates, free α, α2β complex and premature core, the expression of rpoB +C+operon measured by the rate of β subunit synthesis was considerably inhibited whereas that of EF(translation elongation factor)-Tu, ribosomal proteins L1 and L7/L12, and some λ-coded proteins remained unaffected. On the other hand, the expression was enhanced specifically for only rpoB +C+operon in either rpoC4 or rpoC1 mutants, which are defective in the association of α2β complex and β′ subunit or the activation of premature core enzyme, respectively. Upon preincubation of the mutant cells at 42° C prior to phage infection, during which assembly intermediates degraded rapidly, the rate of β subunit synthesis relative to other phage-corded proteins increased remarkably in rpoB2·rpoB7 mutant as well as in rpoC4 and rpoC1 mutants. These observations strongly suggested the autogenous regulation for at least ββ′ (rpoB +C+) operon by some trans-active diffusible protein complexes built of RNA polymerase subunits. Nature of the regulatory molecules is discussed.
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Communicated by E. Bautz
Paper VI in this series is Saitoh and Ishihama (1977)
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Taketo, M., Fukuda, R. & Ishihama, A. Biosynthesis of RNA polymerase in Escherichia coli . Molec. Gen. Genet. 165, 7–14 (1978). https://doi.org/10.1007/BF00270370
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DOI: https://doi.org/10.1007/BF00270370