The RNase P of acterial, called the C5 protein, a component 2, RNA chain, which is known as protein or polypeptide chain and M1 RNA. In vivo, it is necessary for ribozyme both components to function properly, it can act as a catalyst in the M1 RNA in vitro. By increasing the affinity of the metal ion in the active site, the main role of C5 protein to improve the catalytic rate of M1 RNA and enzyme binding affinity of the substrate probably. shows a method according to the shape selective recognition of the target pre-mRNA, the crystal structure of RNase P and bacterial holoenzim mRNA was solved placed helical domain of large coaxial RNase P RNA of recently. The crystal structure shows the location of the active site to verify the earlier models and catalyst substrate recognition, protein component shows a method of increasing the RN RNase P function.

Ribonuclease P (RN RNase P) is a ubiquitous endoribonuclease, found archaea, eukaryotes and bacteria as mitochondria and chloroplasts. Features activities its best is the production of the 5 ‘end of mature tRNA by cutting the leader element 5’ of the precursor tRNA. Ribonucleic RNase Ps of Mobile is (RNP). That is, RNA shell RNase Ps bacterial holding ribozyme catalytic activity in the absence of protein subunits. The RN RNase P RNA of archaebacteria and eukaryotes isolated, it retains its catalytic function is shown, it is still essential for catalytic activity of holoenzim. To Yu protein content very high ones of bacteria of the RNA core, but it has the same phase three lines corresponding to the P1, P2, and spiral,, archaea holoenzyme and eukaryotic organisms and P10 P3, P4 / 11, I is common to RN RNase P RNA of all cells. However, there is considerable variation between the eukaryotic RNA sequence in particular.

In archaea, RN RNase P is made from ribonucleic 4-5 protein subunits that are associated with the RNA. The protein subunits are indicated by the results of in vitro dissolution tests as, mRNA is substantially RNA-mediated component is individually unsuitable for processing. [8] [9] Clearly, X-ray crystallography and determined by NMR new protein domains whereby structure of the protein subunits RN RNase P [10] archaea are essential for function fold . The RN RNase P RNA eukaryotic isolated, it is possible to retain its catalytic function is shown, it is still essential for catalytic activity of holoenzim. To Yu protein content very high ones of bacteria of the RNA core, but it has the same phase three lines corresponding to the P1, P2, and spiral,, archaea holoenzyme and eukaryotic organisms and P10 P3, P4 / 11, I is common to RN RNase P RNA of all cells. However, there is considerable variation between the eukaryotic RNA sequence in particular.

Genus Pyrobaculum, form to use the calculation method of improvement and comparative genomics of RNase P RNA of called “type T”, is minimized fundamentally, Clen archaea family system, including the species Vulcanisaeta and Caldivirga It is found in the complete genome of all of Thermoproteaceae within. Keep the catalytic domain of conventional but there is no specificity of a recognizable domain. Confirmed experimentally processing activities 5 ‘tRNA single RNA. In the form that you discovered that Caldivirga ribonuclease P RNA and Pyrobaculum to function as a trans-acting ribozyme still, naturally occurring minimum. The potential loss of specificity domains in RNA These suggest that substrate specificity is altered.  But lacks the experiment and research archaebacteriium Nanoarchaeum equitans ribonuclease P. computer recently, but insisted that it was not able to find evidence of its existence. Is this organism promoter mRNA, close to the gene mRNA, are thinking about starting from the first base of the mRNA to eliminate the requirement of RNase P RN transcription follow it

AT-RN RNase P is structurally similar to that of the 9-10 binding protein and bacteria (as opposed to RNase P protein of bacteria, such as, and C5) in eukaryotes such as yeast and human like this It consists of a chain RNA you have. Five of the protein subunits of these shows the correspondence of the same sex archaea. Protein subunit of RNase P RN These are shared RN RNase MRP, a ribonucleoprotein catalyst involved in the processing of ribosomal RNA in the nucleolus. The RN RNase P, it is a very recent ribozyme has been shown from eukaryotes. Therefore, processing of tRNA itself has a negligible role of RNase P protein subunit eucaryal many, but they RNase in settings other biologically, such as cell cycle and transcription of such genes It appears to be essential to the function of RNase MRP and P. The bacterial origin of mitochondria and chloroplasts, pigments and animals higher plants, do not appear to include RN RNase P RNA-based, but it, RNase P of human mitochondrial is a protein, RNA does not contain It has been shown. Further RNase P of chloroplasts spinach, can function without subunit RNA is shown.