title: The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.
abstract: Ribonuclease P (RNase P) is an essential endonuclease responsible for catalyzing 5' end maturation in precursor transfer RNAs. Since its discovery in the 1970s, RNase P enzymes have been identified and studied throughout the three domains of life. Interestingly, RNase P is either RNA-based, with a catalytic RNA subunit, or a protein-only (PRORP) enzyme with differential evolutionary distribution. The available structural data, including the active site data, provides insight into catalysis and substrate recognition. The hydrolytic and kinetic mechanisms of the two forms of RNase P enzymes are similar, yet features unique to the RNA-based and PRORP enzymes are consistent with different evolutionary origins. The various RNase P enzymes, in addition to their primary role in tRNA 5' maturation, catalyze cleavage of a variety of alternative substrates, indicating a diversification of RNase P function in vivo. The review concludes with a discussion of recent advances and interesting research directions in the field.
authors.affiliation: Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. klemmbp@umich.edu.
authors.forename: Bradley P
authors.initials: BP
authors.lastname: Klemm
authors.affiliation: Program in Chemical Biology, University of Michigan, Ann Arbor, MI 48109, USA. nancywu@umich.edu.
authors.forename: Nancy
authors.initials: N
authors.lastname: Wu
authors.affiliation: Department of Chemistry, University of Michigan, Ann Arbor, MI 48103, USA. yyuchen@umich.edu.
authors.forename: Yu
authors.initials: Y
authors.lastname: Chen
authors.affiliation: Department of Chemistry, University of Michigan, Ann Arbor, MI 48103, USA. chemxliu@umich.edu.
authors.forename: Xin
authors.initials: X
authors.lastname: Liu
authors.affiliation: Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. kaitanyk@umich.edu.
authors.forename: Kipchumba J
authors.initials: KJ
authors.lastname: Kaitany
authors.affiliation: Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. mhowa@umich.edu.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Howard
authors.affiliation: Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. fierke@umich.edu.|Program in Chemical Biology, University of Michigan, Ann Arbor, MI 48109, USA. fierke@umich.edu.|Department of Chemistry, University of Michigan, Ann Arbor, MI 48103, USA. fierke@umich.edu.
authors.forename: Carol A
authors.initials: CA
authors.lastname: Fierke
mesh_terms: D000818:Animals; D001105:Archaea / Q000235:genetics / Q000378:metabolism; D001419:Bacteria / Q000235:genetics / Q000378:metabolism; D002384:Catalysis; D020134:Catalytic Domain; D006801:Humans; D009690:Nucleic Acid Conformation; D016337:RNA, Catalytic / Q000378:metabolism*; D012343:RNA, Transfer / Q000378:metabolism; D043262:Ribonuclease P / Q000737:chemistry / Q000378:metabolism*
chemical_list: D016337:RNA, Catalytic; D012343:RNA, Transfer; D043262:Ribonuclease P
keywords: PRORP; RNase P; endonuclease; ribozyme; tRNA maturation; tRNA recognition