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Biomolecules 2016, 6(2), 27; doi:10.3390/biom6020027

The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions

1
Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA
2
Program in Chemical Biology, University of Michigan, Ann Arbor, MI 48109, USA
3
Department of Chemistry, University of Michigan, Ann Arbor, MI 48103, USA
Current address: Department of Chemistry, Stanford University, Palo Alto, CA 94305, USA
Current address: National Institute of Environmental Health Sciences, Durham, NC 27713, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Denis Drainas
Received: 21 March 2016 / Revised: 4 May 2016 / Accepted: 6 May 2016 / Published: 13 May 2016
(This article belongs to the Special Issue Function and Structure of RNase P in Fungi, Bacteria and Human Cells)
View Full-Text   |   Download PDF [5476 KB, uploaded 13 May 2016]   |  

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. View Full-Text
Keywords: RNase P; ribozyme; PRORP; endonuclease; tRNA maturation; tRNA recognition RNase P; ribozyme; PRORP; endonuclease; tRNA maturation; tRNA recognition
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Klemm, B.P.; Wu, N.; Chen, Y.; Liu, X.; Kaitany, K.J.; Howard, M.J.; Fierke, C.A. The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions. Biomolecules 2016, 6, 27.

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