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Localization of the Escherichia coli RNA Polymerase ß' Subunit Residue Phosphorylated by Bacteriophage T7 Kinase Gp0.7

Waksman Institute, Piscataway, New Jersey 08854,¹ Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854,² Institute of Molecular Genetics, Russian Academy of Sciences, Moscow 142292, Russia³

Received 5 January 2006/ Accepted 27 February 2006

During bacteriophage T7 infection, the Escherichia coli RNA polymerase ß' 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, Thr¹⁰⁶⁸, in the evolutionarily hypervariable segment of ß'. Using a phosphomimetic substitution of Thr¹⁰⁶⁸, we show that phosphorylation of ß' leads to increased -dependent transcription termination, which may help to switch from host to viral RNA polymerase transcription during phage development.

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