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During bacteriophage T7 infection, the Escherichia coli RNA polymerase beta' subunit is phosphorylated by the phage-encoded kinase Gp0.7. Here, we used proteolytic degradation and mutational analysis to localize the phosphorylation site to a single amino acid, Thr(1068), in the evolutionarily hypervariable segment of beta'. Using a phosphomimetic substitution of Thr(1068), we show that phosphorylation of beta' leads to increased rho-dependent transcription termination, which may help to switch from host to viral RNA polymerase transcription during phage development.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1482854PMC
http://dx.doi.org/10.1128/JB.188.10.3470-3476.2006DOI Listing

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