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Review
. 2002:71:165-89.
doi: 10.1146/annurev.biochem.71.110601.135352. Epub 2001 Nov 9.

Eukaryotic ribonuclease P: a plurality of ribonucleoprotein enzymes

Shaohua Xiao  1 , Felicia Scott, Carol A Fierke, David R Engelke
Affiliations
Review

Eukaryotic ribonuclease P: a plurality of ribonucleoprotein enzymes

Shaohua Xiao et al. Annu Rev Biochem. 2002.

Abstract

Ribonuclease P (RNase P) is an essential endonuclease that acts early in the tRNA biogenesis pathway. This enzyme catalyzes cleavage of the leader sequence of precursor tRNAs (pre-tRNAs), generating the mature 5' end of tRNAs. RNase P activities have been identified in Bacteria, Archaea, and Eucarya, as well as organelles. Most forms of RNase P are ribonucleoproteins, i.e., they consist of an essential RNA subunit and protein subunits, although the composition of the enzyme in mitochondria and chloroplasts is still under debate. The recent purification of the eukaryotic nuclear RNase P has demonstrated a significantly larger protein content compared to the bacterial enzyme. Moreover, emerging evidence suggests that the eukaryotic RNase P has evolved into at least two related nuclear enzymes with distinct functions, RNase P and RNase MRP. Here we review current information on RNase P, with emphasis on the composition, structure, and functions of the eukaryotic nuclear holoenzyme, and its relationship with RNase MRP.

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Figures

Figure 1
Figure 1
Summary of the yeast two-hybrid and three-hybrid test results of yeast (S. cerevisiae) nuclear RNase P. Ovals represent the protein subunits of yeast nuclear RNase P (Table 1). Overlaps of the ovals indicate a positive result in the two-hybrid test (141a). The shaded ovals of Pop1p and Pop4p indicate that they are the only protein subunits that interact specifically with the RPR1 RNA in a three-hybrid test. One of the recognition sites in the RPR1 RNA for Pop1p binding is the P3 loop, as indicated by the arrow (116). The binding sites for Pop4p are currently unknown, which is represented by the dotted bracket and a question mark. The predicted secondary structure of RPR1 RNA is adapted from the model proposed by Frank et al (15). Five critical regions, CR-I to CR-V, are numbered based on the Chen & Pace nomenclature (14). P represents helical regions, with numbers assigned according to the bacterial structure (101). eP indicates the eukaryotic paired regions whose homology to particular bacterial structures is uncertain, but which occupy the same positions as in the bacterial structure (15). Nucleotides in filled circles show protection from chemical modification and nuclease attack in the holoenzyme, whereas the nucleotides in open circles indicate exposure to solution (16).
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