Abstract
We analyzed modes of action of ribonuclease P (RNase P) proteins, C5 in Escherichia coli and Rpr2 in Saccharomyces cerevisiae, using a pair of complementary fluorescence-labeled oligoribonucleotides. Fluorescence resonance energy transfer-based assays revealed that RNA annealing and strand displacement activities found in archaeal RNase P proteins are prevalent in eubacterial (C5) and eukaryotic (Rpr2) RNase P proteins.
| Original language | English |
|---|---|
| Pages (from-to) | 1700-1702 |
| Number of pages | 3 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 78 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - 2014 |
All Science Journal Classification (ASJC) codes
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry
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Furutani, T., Hazeyama, K., Ueda, T., Tomita, S., Imai, T., Nakashima, T., Kakuta, Y., & Kimura, M. (2014). Enhancement of RNA annealing and strand displacement found in archaeal ribonuclease P proteins is conserved in Escherichia coli protein C5 and yeast protein Rpr2. Bioscience, Biotechnology and Biochemistry, 78(10), 1700-1702. https://doi.org/10.1080/09168451.2014.925780