| Bacterial RNase P class A | |
|---|---|
 Predicted secondary structure and sequence conservation of RNaseP_bact_a | |
| Identifiers | |
| Symbol | RNaseP_bact_a |
| Rfam | RF00010 |
| Other data | |
| RNA type | Gene; ribozyme |
| Domain(s) | Bacteria |
| GO | GO:0008033 GO:0004526 GO:0030680 |
| SO | SO:0000386 |
| PDB structures | PDBe |
| Bacterial RNase P class B | |
|---|---|
 Predicted secondary structure and sequence conservation of RNaseP_bact_b | |
| Identifiers | |
| Symbol | RNaseP_bact_b |
| Rfam | RF00011 |
| Other data | |
| RNA type | Gene; ribozyme |
| Domain(s) | Bacteria |
| GO | GO:0008033 GO:0004526 GO:0030680 |
| SO | SO:0000386 |
| PDB structures | PDBe |
| Archaeal RNase P | |
|---|---|
 Predicted secondary structure and sequence conservation of Archaeal RNase P | |
| Identifiers | |
| Symbol | RNaseP_arch |
| Rfam | RF00373 |
| Other data | |
| RNA type | Gene; ribozyme |
| Domain(s) | Archaea |
| GO | GO:0008033 GO:0004526 GO:0030680 |
| SO | SO:0000386 |
| PDB structures | PDBe |
| Archaeal RNase P class T | |
|---|---|
| Identifiers | |
| Symbol | RNaseP-T |
| Rfam | RF02357 |
| Other data | |
| RNA type | Gene; ribozyme |
| Domain(s) | Archaea |
| GO | GO:0008033 GO:0004526 GO:0030680 |
| SO | SO:0000386 |
| PDB structures | PDBe |
Ribonuclease P (EC 3.1.26.5, RNase P) is a type of ribonuclease which cleaves RNA. RNase P is unique from other RNases in that it is a ribozyme – a ribonucleic acid that acts as a catalyst in the same way that a protein-based enzyme would. Its function is to cleave off an extra, or precursor, sequence of RNA on tRNA molecules.[1] Further, RNase P is one of two known multiple turnover ribozymes in nature (the other being the ribosome), the discovery of which earned Sidney Altman and Thomas Cech the Nobel Prize in Chemistry in 1989: in the 1970s, Altman discovered the existence of precursor tRNA with flanking sequences and was the first to characterize RNase P and its activity in processing of the 5' leader sequence of precursor tRNA. Recent findings also reveal that RNase P has a new function.[2] It has been shown that human nuclear RNase P is required for the normal and efficient transcription of various small noncoding RNAs, such as tRNA, 5S rRNA, SRP RNA and U6 snRNA genes,[3] which are transcribed by RNA polymerase III, one of three major nuclear RNA polymerases in human cells.
- ^ Guerrier-Takada C, Gardiner K, Marsh T, Pace N, Altman S (December 1983). "The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme". Cell. 35 (3 Pt 2): 849–57. doi:10.1016/0092-8674(83)90117-4. PMID 6197186. S2CID 39111511.
- ^ Jarrous N, Reiner R (2007). "Human RNase P: a tRNA-processing enzyme and transcription factor". Nucleic Acids Research. 35 (11): 3519–24. doi:10.1093/nar/gkm071. PMC 1920233. PMID 17483522.
- ^ Reiner R, Ben-Asouli Y, Krilovetzky I, Jarrous N (June 2006). "A role for the catalytic ribonucleoprotein RNase P in RNA polymerase III transcription". Genes & Development. 20 (12): 1621–35. doi:10.1101/gad.386706. PMC 1482482. PMID 16778078.