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

Philipp Konrad Zuber, Kristian Schweimer, Paul Rösch, Irina Artsimovitch () and Stefan H. Knauer ()
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Philipp Konrad Zuber: Universität Bayreuth, Universitätsstraße 30
Kristian Schweimer: Universität Bayreuth, Universitätsstraße 30
Paul Rösch: Universität Bayreuth, Universitätsstraße 30
Irina Artsimovitch: The Ohio State University
Stefan H. Knauer: Universität Bayreuth, Universitätsstraße 30

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-08567-6

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