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Ribonuclease P: the evolution of an ancient RNA enzyme Walker SC; Engelke DRCrit Rev Biochem Mol Biol 2006[Mar]; 41 (2): 77-102Ribonuclease P (RNase P) is an ancient and essential endonuclease that catalyses the cleavage of the 5' leader sequence from precursor tRNAs (pre-tRNAs). The enzyme is one of only two ribozymes which can be found in all kingdoms of life (Bacteria, Archaea, and Eukarya). Most forms of RNase P are ribonucleoproteins; the bacterial enzyme possesses a single catalytic RNA and one small protein. However, in archaea and eukarya the enzyme has evolved an increasingly more complex protein composition, whilst retaining a structurally related RNA subunit. The reasons for this additional complexity are not currently understood. Furthermore, the eukaryotic RNase P has evolved into several different enzymes including a nuclear activity, organellar activities, and the evolution of a distinct but closely related enzyme, RNase MRP, which has different substrate specificities, primarily involved in ribosomal RNA biogenesis. Here we examine the relationship between the bacterial and archaeal RNase P with the eukaryotic enzyme, and summarize recent progress in characterizing the archaeal enzyme. We review current information regarding the nuclear RNase P and RNase MRP enzymes in the eukaryotes, focusing on the relationship between these enzymes by examining their composition, structure and functions.|*Evolution, Molecular[MESH]|Animals[MESH]|Base Sequence[MESH]|Humans[MESH]|Models, Biological[MESH]|Molecular Sequence Data[MESH]|Nucleic Acid Conformation[MESH]|Protein Binding[MESH]|RNA Precursors/metabolism[MESH]|Ribonuclease P/chemistry/genetics/*metabolism[MESH]|Ribonucleoproteins/*metabolism[MESH]|Substrate Specificity[MESH] |
