Differential Local Stability Governs the Metamorphic Fold Switch of Bacterial Virulence Factor RfaH.

ABSTRACT: RfaH, a two-domain protein from a universally conserved NusG/Spt5 family of regulators, is required for the transcription and translation of long virulence and conjugation operons in many Gram-negative bacterial pathogens. Escherichia coli RfaH action is controlled by a unique large-scale structural rearrangement triggered by recruitment to transcription elongation complexes through a specific DNA element. Upon recruitment, the C-terminal domain of RfaH refolds from an α-hairpin, which is bound to RNA polymerase binding site within the N-terminal domain, into an unbound β-barrel that interacts with the ribosome. Although structures of the autoinhibited (α-hairpin) and active (β-barrel) states and plausible refolding pathways have been reported, how this reversible switch is encoded within

SUBMITTER: Galaz-Davison P 

PROVIDER: S-EPMC6950767 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature