Of proteins and RNA: the RNase P/MRP family.
Nuclear ribonuclease (RNase) P is a ubiquitous essential ribonucleoprotein complex, one of only two known RNA-based enzymes found in all three domains of life. The RNA component is the catalytic moiety of RNases P across all phylogenetic domains; it contains a well-conserved core, whereas peripheral structural elements are diverse. RNA components of eukaryotic RNases P tend to be less complex than their bacterial counterparts, a simplification that is accompanied by a dramatic reduction of their catalytic ability in the absence of protein. The size and complexity of the protein moieties increase dramatically from bacterial to archaeal to eukaryotic enzymes, apparently reflecting the delegation of some structural functions from RNA to proteins and, perhaps, in response to the increased complexity of the cellular environment in the more evolutionarily advanced organisms; the reasons for the increased dependence on proteins are not clear. We review current information on RNase P and the closely related universal eukaryotic enzyme RNase MRP, focusing on their functions and structural organization.
Esakova
Olga
O
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Krasilnikov
Andrey S
AS
D000818:Animals; D001419:Bacteria / Q000201:enzymology; D004722:Endoribonucleases / Q000737:chemistry* / Q000378:metabolism*; D019143:Evolution, Molecular; D006801:Humans; D043262:Ribonuclease P / Q000737:chemistry* / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000737:chemistry / Q000378:metabolism
D012261:Ribonucleoproteins; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; D043262:Ribonuclease P