Structural basis of transcription arrest by coliphage HK022 Nun in an Escherichia coli RNA polymerase elongation complex

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Coliphage HK022 Nun blocks superinfection by coliphage lambda, by stalling RNA polymerase (RNAP) translocation specifically on lambda, DNA. To provide a structural framework to understand how Nun blocks RNAP translocation, we determined structures of Escherichia coli RNAP ternary elongation complexes (TECs) with and without Nun by single-particle cryo-electron microscopy. Nun fits tightly into the TEC by taking advantage of gaps between the RNAP and the nucleic acids. The C-terminal segment of Nun interacts with the RNAP beta and beta' subunits inside the RNAP active site cleft as well as with nearly every element of the nucleic acid scaffold, essentially crosslinking the RNAP and the nucleic acids to prevent translocation, a mechanism supported by the effects of Nun amino acid substitutions. The nature of Nun interactions inside the RNAP active site cleft suggests that RNAP clamp opening is required for Nun to establish its interactions, explaining why Nun acts on paused TECs.
Publisher
ELIFE SCIENCES PUBLICATIONS LTD
Issue Date
2017-03
Language
English
Article Type
Article
Citation

ELIFE, v.6

ISSN
2050-084X
DOI
10.7554/eLife.25478
URI
http://hdl.handle.net/10203/251675
Appears in Collection
CH-Journal Papers(저널논문)
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