Fig. 7: Modulating ρ activity by oligomerization.
From: Nucleotide-induced hyper-oligomerization inactivates transcription termination factor ρ
a Schematic diagrams of ρ proteins from representative bacteria. The IDR/prion-like domains with predicted local distance difference test (plDDT; see “Methods”) < 50 modeled by AlphaFold 3 are shown as orange/magenta bars. b The ring conformation controls ρ activity; an open inactive hexamer can be stabilized by accessory proteins, such as Rof and YihE (not shown; see text for details) or trapped by ligand-induced polymerization/filamentation, as we observed with E. coli ρ. Formation of amyloids, whose structures remain to be determined, inactivates C. botulinum ρ, whereas phase separation increases ρ activity in B. thetaiotaomicron.
