A distinct binding mode of archaeal ribonuclease P proteins to RNA.

Masato Ishihara, Etsuko Nishimoto, Shoji Yamashita, Yoshimitsu Kakuta, Makoto Kimura

Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.

Bioscience, biotechnology, and biochemistry 2012

filter terms:

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.

Citation

Masato Ishihara, Etsuko Nishimoto, Shoji Yamashita, Yoshimitsu Kakuta, Makoto Kimura. A distinct binding mode of archaeal ribonuclease P proteins to RNA. Bioscience, biotechnology, and biochemistry. 2012;76(12):2335-7