Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 76, Issue 12, Pages 2335-2337Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.120546
Keywords
fluorescence resonance energy transfer; Pyrococcus horikoshii; RNA-binding protein; RNA chaperon; ribonuclease P proteins
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [22380062]
- Grants-in-Aid for Scientific Research [22380062] Funding Source: KAKEN
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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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