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The composition of RNase P varies across the three domains of life and therefore may afford high selectivity in drug targeting. While in archaea and eukaryotes, RNase P is comprised of one RNA subunit and four to ten proteins, in bacteria, this complex is formed by an RNA subunit (P RNA, 350–400 nucleotides, 110–125 kDa) and a single protein (P protein, ∼110 amino acids, 13 kDa). In all species, the P RNA can serve as the primary biocatalyst for the cleavage of the 5′-leader sequence of pre-tRNAs during tRNA maturation. The P protein, on the other hand, can bind the distal 5′-leader region of the pre-tRNA substrate, enhances the affinity of metal ions, and assists in product release. And RNase P is dependent on divalent metal ions (Mg2+ is needed for proper folding and activity and in vitro, high concentrations of Mg2+ are sufficient to allow P RNA catalysis, even in the absence of the protein subunit.