title: Structural studies of RNase P.
abstract: Ribonuclease P (RNase P) is one of the first ribozymes discovered and it is found in all phylogenetic groups. It is responsible for processing the 5' end of pre-tRNAs as well as other RNA molecules. RNase P is formed by an RNA molecule responsible for catalysis and one or more proteins. Structural studies of the proteins from different organisms, the bacterial RNA component, and a bacterial RNase P holoenzyme/tRNA complex provide insights into the mechanism of this universal ribozyme. Together with the existing wealth of biochemical information, these studies provide atomic-level information on the mechanism of RNase P and continue to expand our understanding of the structure and architecture of large RNA molecules and ribonucleoprotein complexes, the nature of catalysis by ribozymes, the structural basis of recognition of RNA by RNA molecules, and the evolution of enzymes from the prebiotic, RNA-based world to the modern world.
authors: Department of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA. a-mondragon@northwestern.edu
authors: Alfonso
authors: A
authors: Mondragón
mesh_terms: D000818:Animals; D001419:Bacteria / Q000201:enzymology / Q000235:genetics; D002384:Catalysis; D056890:Eukaryota / Q000201:enzymology / Q000235:genetics; D020035:Holoenzymes / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D010802:Phylogeny; D043262:Ribonuclease P / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D020035:Holoenzymes; D043262:Ribonuclease P