A Distinct Binding Mode of Archaeal Ribonuclease P Proteins to RNA

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  • ISHIHARA Masato
    Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University
  • NISHIMOTO Etsuko
    Institute of Biophysics, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University
  • YAMASHITA Shoji
    Institute of Biophysics, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University
  • KAKUTA Yoshimitsu
    Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University
  • KIMURA Makoto
    Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University

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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.

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