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  Structural Basis for the Action of an All-Purpose Transcription Anti-termination Factor

Krupp, F., Said, N., Huang, Y.-H., Loll, B., Bürger, J., Mielke, T., et al. (2019). Structural Basis for the Action of an All-Purpose Transcription Anti-termination Factor. Molecular Cell, 74(1): e5, pp. 143-157. doi:10.1016/j.molcel.2019.01.016.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-568F-C Version Permalink: http://hdl.handle.net/21.11116/0000-0003-5690-9
Genre: Journal Article

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 Creators:
Krupp, Ferdinand , Author
Said, Nelly , Author
Huang, Yong-Heng , Author
Loll, Bernhard, Author
Bürger, Jörg1, Author              
Mielke, Thorsten1, Author              
Spahn, Christian M.T. , Author
Wahl, Markus C. , Author
Affiliations:
1Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              

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Free keywords: N proteins of lambdoid phages; Nus factors; RNA polymerase regulation; intrinsic transcription termination; processive transcription anti-termination; single-particle cryo-electron microscopy; structural biology; transcription regulation; transcriptional pausing; ρ-dependent transcription termination
 Abstract: Bacteriophage λN protein, a model anti-termination factor, binds nascent RNA and host Nus factors, rendering RNA polymerase resistant to all pause and termination signals. A 3.7-Å-resolution cryo-electron microscopy structure and structure-informed functional analyses reveal a multi-pronged strategy by which the intrinsically unstructured λN directly modifies RNA polymerase interactions with the nucleic acids and subverts essential functions of NusA, NusE, and NusG to reprogram the transcriptional apparatus. λN repositions NusA and remodels the β subunit flap tip, which likely precludes folding of pause or termination RNA hairpins in the exit tunnel and disrupts termination-supporting interactions of the α subunit C-terminal domains. λN invades and traverses the RNA polymerase hybrid cavity, likely stabilizing the hybrid and impeding pause- or termination-related conformational changes of polymerase. λN also lines upstream DNA, seemingly reinforcing anti-backtracking and anti-swiveling by NusG. Moreover, λN-repositioned NusA and NusE sequester the NusG C-terminal domain, counteracting ρ-dependent termination. Other anti-terminators likely utilize similar mechanisms to enable processive transcription.

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Language(s): eng - English
 Dates: 2019-02-192019-04-04
 Publication Status: Published in print
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 Rev. Method: -
 Identifiers: DOI: 10.1016/j.molcel.2019.01.016
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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: 15 Volume / Issue: 74 (1) Sequence Number: e5 Start / End Page: 143 - 157 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929