A distinct binding mode of archaeal ribonuclease P proteins to RNA

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

Research output: Contribution to journalArticle

7 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2335-2337
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume76
Issue number12
DOIs
Publication statusPublished - Dec 1 2012

Fingerprint

Pyrococcus horikoshii
Ribonuclease P
Oligoribonucleotides
RNA
Fluorescence Resonance Energy Transfer
RNA-Binding Proteins
Archaea
Proteins
Fluorescence
Conformations
Assays

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Cite this

A distinct binding mode of archaeal ribonuclease P proteins to RNA. / Ishihara, Masato; Nishimoto, Etsuko; Yamashita, Shoji; Kakuta, Yoshimitsu; Kimura, Makoto.

In: Bioscience, Biotechnology and Biochemistry, Vol. 76, No. 12, 01.12.2012, p. 2335-2337.

Research output: Contribution to journalArticle

Ishihara, Masato ; Nishimoto, Etsuko ; Yamashita, Shoji ; Kakuta, Yoshimitsu ; Kimura, Makoto. / A distinct binding mode of archaeal ribonuclease P proteins to RNA. In: Bioscience, Biotechnology and Biochemistry. 2012 ; Vol. 76, No. 12. pp. 2335-2337.
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