A Distinct Binding Mode of Archaeal Ribonuclease P Proteins to RNA

The ribonuclease P (RNase P) in the hyperthermophilic archaeon Pyrococcus horikoshii comprises RNA (PhopRNA) and five proteins. We analyzed the RNA binding mode of the protein, using a pair of complementary fluorescence-labeled oligoribonucleotides. Fluorescence resonance energy transfer (FRET)-based assays suggested that the RNase P proteins assist PhopRNA in attaining a functionally active conformation via a distinct mode of binding.