title: A distinct binding mode of archaeal ribonuclease P proteins to RNA.
abstract: 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.
authors.affiliation: Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
authors.forename: Masato
authors.initials: M
authors.lastname: Ishihara
authors.forename: Etsuko
authors.initials: E
authors.lastname: Nishimoto
authors.forename: Shoji
authors.initials: S
authors.lastname: Yamashita
authors.forename: Yoshimitsu
authors.initials: Y
authors.lastname: Kakuta
authors.forename: Makoto
authors.initials: M
authors.lastname: Kimura
mesh_terms: D031541:Fluorescence Resonance Energy Transfer; D011485:Protein Binding; D043902:Pyrococcus horikoshii / Q000201:enzymology*; D019642:RNA, Archaeal / Q000378:metabolism*; D043262:Ribonuclease P / Q000378:metabolism*
chemical_list: D019642:RNA, Archaeal; D043262:Ribonuclease P