Full shut-off of Escherichia coli RNA-polymerase by T7 phage requires a small phage-encoded DNA-binding protein

Aline Tabib-Salazar, Bing Liu, Andrey Shadrin, Lynn Burchell, Zhexin Wang, Zhihao Wang, Moran G. Goren, Ido Yosef, Udi Qimron, Konstantin Severinov, Steve J. Matthews, Sivaramesh Wigneshweraraj

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Infection of Escherichia coli by the T7 phage leads to rapid and selective inhibition of the bacterial RNA polymerase (RNAP) by the 7 kDa T7 protein Gp2. We describe the identification and functional and structural characterisation of a novel 7 kDa T7 protein, Gp5.7, which adopts a winged helix-turn-helix-like structure and specifically represses transcription initiation from host RNAP-dependent promoters on the phage genome via a mechanism that involves interaction with DNA and the bacterial RNAP. Whereas Gp2 is indispensable for T7 growth in E. coli, we show that Gp5.7 is required for optimal infection outcome. Our findings provide novel insights into how phages fine-tune the activity of the host transcription machinery to ensure both successful and efficient phage progeny development.

Original languageEnglish
Pages (from-to)7697-7707
Number of pages11
JournalNucleic Acids Research
Volume45
Issue number13
DOIs
StatePublished - 1 Jul 2017
Externally publishedYes

ASJC Scopus subject areas

  • Genetics

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