Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 110, Issue 49, Pages 19772-19777Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1314576110
Keywords
bacteriophage T7 Gp2; X-ray crystallography; transcription
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Funding
- US Department of Energy, Office of Basic Energy Sciences
- National Center for Research Resources at the National Institutes of Health (NIH) [RR-15301]
- Merck Postdoctoral Fellowship (The Rockefeller University)
- National Research Service Award [NIH F32 GM103170]
- Biotechnology and Biological Sciences Research Council Project Grant [BB/K000233/1]
- BBSRC [BB/K000233/1] Funding Source: UKRI
- MRC [MR/J006874/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/K000233/1] Funding Source: researchfish
- Wellcome Trust [100958/Z/13/Z] Funding Source: researchfish
- Wellcome Trust [100958/Z/13/Z] Funding Source: Wellcome Trust
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Bacteriophage T7 encodes an essential inhibitor of the Escherichia coli host RNA polymerase (RNAP), the product of gene 2 (Gp2). We determined a series of X-ray crystal structures of E. coli RNAP holoenzyme with or without Gp2. The results define the structure and location of the RNAP sigma(70) subunit domain 1.1 (sigma(70)(1.1)) inside the RNAP active site channel, where it must be displaced by the DNA upon formation of the open promoter complex. The structures and associated data, combined with previous results, allow for a complete delineation of the mechanism for Gp2 inhibition of E. coli RNAP. In the primary inhibition mechanism, Gp2 forms a protein-protein interaction with sigma(70)(1.1), preventing the normal egress of sigma(70)(1.1) from the RNAP active site channel. Gp2 thus misappropriates a domain of the RNAP holoenzyme, sigma(70)(1.1), to inhibit the function of the enzyme.
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