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Reversible fold-switching controls the functional cycle of the antitermination factor RfaH

Author

Listed:
  • Philipp Konrad Zuber

    (Universität Bayreuth, Universitätsstraße 30)

  • Kristian Schweimer

    (Universität Bayreuth, Universitätsstraße 30)

  • Paul Rösch

    (Universität Bayreuth, Universitätsstraße 30
    Universität Bayreuth, Universitätsstraße 30)

  • Irina Artsimovitch

    (The Ohio State University
    The Ohio State University)

  • Stefan H. Knauer

    (Universität Bayreuth, Universitätsstraße 30)

Abstract

RfaH, member of the NusG/Spt5 family, activates virulence genes in Gram-negative pathogens. RfaH exists in two states, with its C-terminal domain (CTD) folded either as α-helical hairpin or β-barrel. In free RfaH, the α-helical CTD interacts with, and masks the RNA polymerase binding site on, the N-terminal domain, autoinhibiting RfaH and restricting its recruitment to opsDNA sequences. Upon activation, the domains separate and the CTD refolds into the β-barrel, which recruits a ribosome, activating translation. Using NMR spectroscopy, we show that only a complete ops-paused transcription elongation complex activates RfaH, probably via a transient encounter complex, allowing the refolded CTD to bind ribosomal protein S10. We also demonstrate that upon release from the elongation complex, the CTD transforms back into the autoinhibitory α-state, resetting the cycle. Transformation-coupled autoinhibition allows RfaH to achieve high specificity and potent activation of gene expression.

Suggested Citation

  • Philipp Konrad Zuber & Kristian Schweimer & Paul Rösch & Irina Artsimovitch & Stefan H. Knauer, 2019. "Reversible fold-switching controls the functional cycle of the antitermination factor RfaH," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08567-6
    DOI: 10.1038/s41467-019-08567-6
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    Cited by:

    1. Joseph W. Schafer & Lauren L. Porter, 2023. "Evolutionary selection of proteins with two folds," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Lauren L. Porter & Allen K. Kim & Swechha Rimal & Loren L. Looger & Ananya Majumdar & Brett D. Mensh & Mary R. Starich & Marie-Paule Strub, 2022. "Many dissimilar NusG protein domains switch between α-helix and β-sheet folds," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    3. Philipp K. Zuber & Nelly Said & Tarek Hilal & Bing Wang & Bernhard Loll & Jorge González-Higueras & César A. Ramírez-Sarmiento & Georgiy A. Belogurov & Irina Artsimovitch & Markus C. Wahl & Stefan H., 2024. "Concerted transformation of a hyper-paused transcription complex and its reinforcing protein," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    4. Devlina Chakravarty & Joseph W. Schafer & Ethan A. Chen & Joseph F. Thole & Leslie A. Ronish & Myeongsang Lee & Lauren L. Porter, 2024. "AlphaFold predictions of fold-switched conformations are driven by structure memorization," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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