http://pacelab.colorado.edu/Ppdf/Evans2006.pdf

RNase P: interface of the RNA and protein worlds

Nuclear ribonuclease (RNase) P is a ubiquitous essential ribonucleoprotein complex, one of only two known RNA-based enzymes found in all three domains of life. The RNA component is the catalytic moiety of RNases P across all phylogenetic domains; it contains a well-conserved core, whereas peripheral structural elements are diverse. RNA components of eukaryotic RNases P tend to be less complex than their bacterial counterparts, a simplification that is accompanied by a dramatic reduction of their catalytic ability in the absence of protein. The size and complexity of the protein moieties increase dramatically from bacterial to archaeal to eukaryotic enzymes, apparently reflecting the delegation of some structural functions from RNA to proteins and, perhaps, in response to the increased complexity of the cellular environment in the more evolutionarily advanced organisms; the reasons for the increased dependence on proteins are not clear. We review current information on RNase P and the closely related universal eukaryotic enzyme RNase MRP, focusing on their functions and structural organization.

/pdf/of-proteins-and-rna-the-rnase-p-mrp-family-118v9kszac.pdf

Of proteins and RNA: The RNase P/MRP family

Ribonuclease P (RNase P) is a ubiquitous endonuclease that catalyses the maturation of the 5' end of transfer RNA (tRNA). Although it carries out a biochemically simple reaction, RNase P is a complex ribonucleoprotein particle composed of a single large RNA and at least one protein component. In bacteria and some archaea, the RNA component of RNase P can catalyse tRNA maturation in vitro in the absence of proteins. The discovery of the catalytic activity of the bacterial RNase P RNA triggered numerous mechanistic and biochemical studies of the reactions catalysed by the RNA alone and by the holoenzyme and, in recent years, structures of individual components of the RNase P holoenzyme have been determined. The goal of the present review is to summarize what is known about the bacterial RNase P, and to bring together the recent structural results with extensive earlier biochemical and phylogenetic findings.

Bacterial RNase P: a new view of an ancient enzyme

Ribonuclease P (RNase P) is an ancient and essential endonuclease that catalyses the cleavage of the 5' leader sequence from precursor tRNAs (pre-tRNAs). The enzyme is one of only two ribozymes which can be found in all kingdoms of life (Bacteria, Archaea, and Eukarya). Most forms of RNase P are ribonucleoproteins; the bacterial enzyme possesses a single catalytic RNA and one small protein. However, in archaea and eukarya the enzyme has evolved an increasingly more complex protein composition, whilst retaining a structurally related RNA subunit. The reasons for this additional complexity are not currently understood. Furthermore, the eukaryotic RNase P has evolved into several different enzymes including a nuclear activity, organellar activities, and the evolution of a distinct but closely related enzyme, RNase MRP, which has different substrate specificities, primarily involved in ribosomal RNA biogenesis. Here we examine the relationship between the bacterial and archaeal RNase P with the eukaryotic enzyme, and summarize recent progress in characterizing the archaeal enzyme. We review current information regarding the nuclear RNase P and RNase MRP enzymes in the eukaryotes, focusing on the relationship between these enzymes by examining their composition, structure and functions.

/pdf/ribonuclease-p-the-evolution-of-an-ancient-rna-enzyme-3enkrlkj5h.pdf

Ribonuclease P: The evolution of an ancient RNA enzyme

The enigma of ribonuclease P evolution.

The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA.

This invention relates to a novel bacterial ribonucleoprotein complex and the component parts thereof. More specifically, this invention relates to RNase P RNA isolated from Staphylococcus aureus and the use of RNase P RNA in screens for the identification of antimicrobial compounds and to the use of such compounds in therapy.

Rnase p polypeptides

L'invention concerne un nouveau complexe de ribonucleoproteines bacterien et les elements du compose correspondants. Plus specifiquement, l'invention concerne la RNase P ARN isolee a partir de Staphylococcus aureus et l'utilisation de la RNase P sur des ecrans servant a l'identification de composes antimicrobiens, ainsi que l'utilisation de ces composes en therapie.

Polypeptides rnase p

Publisher Summary
The functional importance of ribonucleic acid (RNA); participating in almost all macromolecular processes, is well established. RNA motifs regulate RNA processing, messenger RNA (mRNA) translation, stability and localization. The most extensively studied RNAs are those that constitute the ribosome, the ribosomal RNA (rRNAs) are critical to both the structure and function of the ribosome during protein synthesis. These are all examples of potential RNA-based targets. Natural inhibitors of protein synthesis are well documented and therefore ribonucleoprotein particles (RNPs) can be considered as valid targets for drug development. Detailed knowledge of the structure and function of any target is a key to understand the mechanism of drug action. RNA participates in almost all macromolecular processes including RNA processing, protein synthesis and protein transport.

Sabine Guth

Papers

The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA.

Rnase p polypeptides

Polypeptides rnase p

6 – Exploiting RNA: Potential Targets, Screens and Drug Development