Rumraket said:Oh by the way, you're going to love this(2 minutes on pubmed can do wonders for your knowledge):
http://www.ncbi.nlm.nih.gov/pubmed/18451863
Life without RNase P.
Abstract
The universality of ribonuclease P (RNase P), the ribonucleoprotein essential for transfer RNA (tRNA) 5' maturation, is challenged in the archaeon Nanoarchaeum equitans. Neither extensive computational analysis of the genome nor biochemical tests in cell extracts revealed the existence of this enzyme. Here we show that the conserved placement of its tRNA gene promoters allows the synthesis of leaderless tRNAs, whose presence was verified by the observation of 5' triphosphorylated mature tRNA species. Initiation of tRNA gene transcription requires a purine, which coincides with the finding that tRNAs with a cytosine in position 1 display unusually extended 5' termini with an extra purine residue. These tRNAs were shown to be substrates for their cognate aminoacyl-tRNA synthetases. These findings demonstrate how nature can cope with the loss of the universal and supposedly ancient RNase P through genomic rearrangement at tRNA genes under the pressure of genome condensation.
Here's an organism living fine without your supposedly absolutely required enzyme.
i already knew about that. Laurence Moran brought it to my knowledge. N. equitans was the first organism to be identified to generate six tRNA isoacceptors via a trans-splicing reaction using tRNA half molecules. So it uses a other mechanism, but it has to splice and cleave the introns together as well. So the need remains.......it can reduce Rnase P, but has to use another reaction, so the mechanism is not really reducable.