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

Abstract

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.

• Authors: Elena Severinova, Konstantin Severinov
• Journal: Journal of bacteriology (J Bacteriol) Vol. 188 Issue 10 Pg. 3470-6 (May 2006) ISSN: 0021-9193 [Print] United States
• PMID: 16672600 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)

Chemical References

• Protein Subunits
• Viral Proteins
• 0.7 protein, Enterobacteria phage T7
• Protein Serine-Threonine Kinases
• DNA-Directed RNA Polymerases
• RNA polymerase beta subunit

Topics

• Amino Acid Sequence
• Bacteriophage T7 (enzymology)
• DNA-Directed RNA Polymerases (chemistry, metabolism)
• Escherichia coli (enzymology)
• Molecular Sequence Data
• Phosphorylation
• Protein Serine-Threonine Kinases (chemistry, metabolism)
• Protein Subunits (metabolism)
• Sequence Alignment
• Sequence Homology, Amino Acid
• Viral Proteins (chemistry, metabolism)