| Comments: |
The enzyme, which is found in archaea, bacteria and eukaryotes, is essential for tRNA processing. It generates 5′-termini or mature tRNA molecules. The enzyme from most sources has been shown to have an RNA chain and a one or more polypeptide chains, but since the RNA chain can act alone as a catalyst in vitro the enzyme should be considered to be a ribozyme [1,2]. Human mitochondrial RNase P has been shown to be a protein that does not require RNA for activity [3]. Spinach chloroplast RNase P has also been shown to function without an RNA component [4]. |
| References: |
| 1. |
Kikovska, E., Svard, S.G. and Kirsebom, L.A. Eukaryotic RNase P RNA mediates cleavage in the absence of protein. Proc. Natl. Acad. Sci. USA 104 (2007) 2062–2067. [DOI] [PMID: 17284611] |
| 2. |
Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N. and Altman, S. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell 35 (1983) 849–857. [DOI] [PMID: 6197186] |
| 3. |
Holzmann, J., Frank, P., Loffler, E., Bennett, K.L., Gerner, C. and Rossmanith, W. RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme. Cell 135 (2008) 462–474. [DOI] [PMID: 18984158] |
| 4. |
Thomas, B.C., Li, X. and Gegenheimer, P. Chloroplast ribonuclease P does not utilize the ribozyme-type pre-tRNA cleavage mechanism. RNA 6 (2000) 545–553. [DOI] [PMID: 10786845] |
|
Printable version