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| Title | Structural basis for protein-free catalysis by ribonuclease P ribozyme. |
|---|---|
| Journal, issue, pages | Nat Commun, Year 2026 |
| Publish date | Apr 15, 2026 |
 Authors | Yun-Tzai Lee / Maximilia F S Degenhardt / Ilias Skeparnias / Szu-Yun Chen / Bapurao A Bhoge / Sergey G Tarasov / Marzena A Dyba / Jinwei Zhang / Jason R Stagno / Yun-Xing Wang /  |
| PubMed Abstract | Ribonuclease P (RNase P) is an essential metallonuclease found in all three domains of life. However, the structural basis for the ancient RNase P RNA component acting alone as a ribozyme and ...Ribonuclease P (RNase P) is an essential metallonuclease found in all three domains of life. However, the structural basis for the ancient RNase P RNA component acting alone as a ribozyme and catalytic metal-ion chemistry remains unknown. We report a series of cryo-EM structures, at resolutions of 2.8-3.5 Å, of the Geobacillus stearothermophilus RNase P aporibozyme (apoE) in various states of the catalytic cycle. The formation of both the tetraloop/tetraloop-receptor interaction and the interdigitated double T-loop motif in the substrate-specificity domain facilitates substrate binding. The apoE uses two metal ions for catalysis, suggesting a catalytic mechanism and evolutionary importance of the RNase P ribozyme to function without its protein component. Together, our data portray the regulatory RNA-RNA interfaces, dynamic structures, and cation traffic that confer function to a trans-acting ribozyme. |
 External links | Nat Commun / PubMed:41986363 |
| Methods | EM (single particle) |
| Resolution | 2.78 - 2.86 Å |
| Structure data | EMDB-70937, PDB-9own: EMDB-70940, PDB-9owq: |
| Chemicals |  ChemComp-CA: |
| Source |
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 Keywords | RNA / ribozyme / RNase P. |
geobacillus stearothermophilus (bacteria)