Dataset Information


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

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.


PROVIDER: S-EPMC6370827 | BioStudies | 2019-01-01


REPOSITORIES: biostudies

Similar Datasets

2013-01-01 | S-EPMC3905879 | BioStudies
2012-01-01 | S-EPMC3430373 | BioStudies
2018-01-01 | S-EPMC5823028 | BioStudies
2015-01-01 | S-EPMC4521827 | BioStudies
2010-01-01 | S-EPMC2871177 | BioStudies
1000-01-01 | S-EPMC2034486 | BioStudies
2007-01-01 | S-EPMC3116145 | BioStudies
2020-01-01 | S-EPMC7593976 | BioStudies
2018-01-01 | S-EPMC6595482 | BioStudies
1000-01-01 | S-EPMC3911127 | BioStudies