Journal
MOLECULAR CELL
Volume 47, Issue 5, Pages 755-766Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2012.06.013
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Funding
- Biotechnology and Biological Sciences Research Council
- Wellcome Trust
- National Institutes of Health [GM59295, GM64530]
- Presidium Molecular and Cellular Biology Program of the Russian Academy of Sciences
- Biotechnology and Biological Sciences Research Council [BB/E023703]
- Biotechnology and Biological Sciences Research Council [BB/E023703/1, BB/K000233/1] Funding Source: researchfish
- BBSRC [BB/K000233/1, BB/E023703/1] Funding Source: UKRI
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The T7 phage-encoded small protein Gp2 is a non-DNA-binding transcription factor that interacts with the jaw domain of the Escherichia coli (Ec) RNA polymerase (RNAp) beta' subunit and inhibits transcriptionally proficient promoter-complex (RPo) formation. Here, we describe the high-resolution solution structure of the Gp2-Ec beta' jaw domain complex and show that Gp2 and DNA compete for binding to the beta' jaw domain. We reveal that efficient inhibition of RPo formation by Gp2 requires the amino-terminal sigma(70) domain region 1.1 (R1.1), and that Gp2 antagonizes the obligatory movement of R1.1 during RPo formation. We demonstrate that Gp2 inhibits RPo formation not just by steric occlusion of the RNAp-DNA interaction but also through long-range antagonistic effects on RNAp-promoter interactions around the RNAp active center that likely occur due to repositioning of R1.1 by Gp2. The inhibition of Ec RNAp by Gp2 thus defines a previously uncharacterized mechanism by which bacterial transcription is regulated by a viral factor.
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