Conversion of Bacillus subtilis RNA polymerase activity in vitro by a protein induced by phage SP01.

A protein fraction from B. subtilis infected with phage SP01 (fraction LGG) stimulates the activity of RNA polymerase (EC 2.7.7.6; nucleosidetriphosphate:RNA nucleotidyltransferase) core from uninfected bacteria. Fraction LGG contains a protein (P-28, molecular weight 28,000) that is labeled after phage infection and binds tightly to RNA polymerase core at a relatively high ionic strength. B. subtilis RNA polymerase core with bound P-28 has the transcription specificity of the previously purified, phage-modified B-P RNA polymerase; the latter contains two subunits, v-28 and v-13 (molecular weights 28,000 and 13,000, respectively) that are synthesized after phage infection. Both enzymes transcribe SP01 DNA preferentially and direct the asymmetric synthesis of viral middle RNA. P-28, like v-28, binds more tightly to B. subtilis RNA polymerase core than the B. subtilis initiation factor, sigma, at higher ionic strength. We propose that P-28 and v-28 are the same protein. P-28 and, by implication, v-28 suffice to endow the bacterial RNA polymerase core with a novel transcription specificity.