Localization of the Escherichia coli RNA polymerase β′ subunit residue phosphorylated by bacteriophage T7 kinase Gp0.7

Elena Severinova, Konstantin Severinov

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)

Abstract

During bacteriophage T7 infection, the Escherichia coli RNA polymerase β′ 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 β′. Using a phosphomimetic substitution of Thr1068, we show that pliosphorylation of β′ leads to increased ρ-dependent transcription termination, which may help to switch from host to viral RNA polymerase transcription during phage development.

Original languageEnglish
Pages (from-to)3470-3476
Number of pages7
JournalJournal of Bacteriology
Volume188
Issue number10
DOIs
Publication statusPublished - May 2006
Externally publishedYes

Fingerprint

Dive into the research topics of 'Localization of the Escherichia coli RNA polymerase β′ subunit residue phosphorylated by bacteriophage T7 kinase Gp0.7'. Together they form a unique fingerprint.

Cite this