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.
Highlights
The 1989 Nobel Prize in Chemistry was awarded to Sidney Altman and Thomas Cech “for their discovery of catalytic properties of RNA” [1]
Two types of Ribonuclease P (RNase P) enzymes exist: (1) RNA-dependent enzymes, for which the active site is located in a catalytic RNA subunit, and (2) protein-only RNase Ps
Footprinting experiments revealed that the RPP21–RPP29 subcomplex contacts the S domain, while the RPP30–POP5 subcomplex contacts the catalytic domain of archaeal RNase P RNA in a position similar to the bacterial protein [39,103]
Summary
The 1989 Nobel Prize in Chemistry was awarded to Sidney Altman and Thomas Cech “for their discovery of catalytic properties of RNA” [1]. Two types of RNase P enzymes exist: (1) RNA-dependent enzymes (ribozymes), for which the active site is located in a catalytic RNA subunit, and (2) protein-only RNase Ps RNase Ps provide the opportunity to compare catalytic strategies of independently evolved protein and RNA catalysts in the only known biological model system in which both are utilized in extant biology to execute the same biological function. 29 the life; the known2016, structures of RNase P enzymes; the catalytic strategies employed by RNase P; substrate recognition recognitionstrategies strategiesofofRNase. Life; the known structures of RNase P enzymes; the catalytic strategies employed by RNase P; and the substrate recognition strategies of RNase P. 1. RNase catalyze metal-dependent, metal‐dependent, endonucleolytic of pre-tRNA pre‐tRNA.
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