Abstract
Ribonuclease P is the endoribonuclease that specifically cleaves precursor sequences from the 5’-ends of pre-tRNAs, to produce the 5’-termini of mature tRNAs. The enzyme is present and essential in all cells and organelles that produce tRNA. RNase P is remarkable because of its composition: it is composed of RNA and protein subunits. The RNA moiety forms the catalytic center, so RNase P is intrinsically a ribozyme. The enzyme from a broad diversity of organisms has been investigated, including representatives of all the phylogenetic domains: Archaea (formerly archaebacteria), Bacteria (formerly eubacteria) and Eucarya (eucaryotes). The properties of RNase P and its reaction have been extensively and recently reviewed (Pace and Smith 1990; Darr et al. 1992; Altman et al. 1993; Pace and Brown 1995). The purpose of this chapter is to provide an overview of the development of our current understanding of the structure of the RNase P RNA. An important key to understanding the function and specificity of this interesting enzyme is to gain perspective on its structure. A detailed secondary structure model of the bacterial RNA has been derived through phylogenetic comparative analysis, and comparative and cross-linking studies are revealing the packing of the secondary structural elements, the global tertiary structure. The resolution of the current tertiary structure model is sufficient to encourage molecular modeling for much of the RNA, based on known atomic-level structures.
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Nolan, J.M., Pace, N.R. (1996). Structural Analysis of the Bacterial Ribonuclease P RNA. In: Eckstein, F., Lilley, D.M.J. (eds) Catalytic RNA. Nucleic Acids and Molecular Biology, vol 10. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-61202-2_6
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DOI: https://doi.org/10.1007/978-3-642-61202-2_6
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