A Distinct Binding Mode of Archaeal Ribonuclease P Proteins to RNA

Masato ISHIHARA; Etsuko NISHIMOTO; Shoji YAMASHITA; Yoshimitsu KAKUTA; Makoto KIMURA

doi:10.1271/bbb.120546

This article has now been updated. Please use the final version.

A Distinct Binding Mode of Archaeal Ribonuclease P Proteins to RNA

Masato ISHIHARA, Etsuko NISHIMOTO, Shoji YAMASHITA, Yoshimitsu KAKUTA, Makoto KIMURA

Author information

Keywords: fluorescence resonance energy transfer, Pyrococcus horikoshii, RNA-binding protein, RNA chaperon, ribonuclease P proteins

JOURNAL FREE ACCESS Advance online publication

Article ID: 120546

DOI https://doi.org/10.1271/bbb.120546

The final version of this article is now available: Vol. 76 (2012) , No. 12 p.2335

Details

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.

Corresponding author

Register with J-STAGE for free!