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Journal of Bacteriology, May 2006, p. 3470-3476, Vol. 188, No. 10
0021-9193/06/$08.00+0     doi:10.1128/JB.188.10.3470-3476.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

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

Elena Severinova1 and Konstantin Severinov1,2,3*

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 {rho}-dependent transcription termination, which may help to switch from host to viral RNA polymerase transcription during phage development.

* Corresponding author. Mailing address: Waksman Institute, 190 Frelinghuysen Road, Piscataway, NJ 08854. Phone: (732) 445-6095. Fax: (732) 445-5735. E-mail: severik{at}waksman.rutgers.edu.

Journal of Bacteriology, May 2006, p. 3470-3476, Vol. 188, No. 10
0021-9193/06/$08.00+0     doi:10.1128/JB.188.10.3470-3476.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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