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This presentation is about RNase P in Archaea. Before describing what we've learned and what we hope to learn about RNase P in Archaea, even before introducing both RNase P and the Archaea, let me pre-emptively tell you why we're interested in RNase P generally, and why you should be interested enough in it to go through this presentation.

First, and foremost for me personally, is that RNase P is a catalytic RNA, or "ribozyme", and is probably a left-over of the very earliest stages in the emergence of life from non-life, the so-called (and hypothetical) "RNA World" stage before the evolutionary invention of either DNA or protein, when RNA carried out both the roles of information storage (genome) and catalytic function (metabolism). RNase P, then, has something to tell us about the biggest question there is for us humans; Where do we come from?

Secondly, as an enzyme, RNase P is a great model system to study how RNA structure works. The functional ramifications of any changes made to the RNA structure can be tested using standard enzymology, something that can't be done with other large RNAs such as the ribosomal RNAs, SRP RNA, tmRNA, etc.

Thirdly, RNase P is a great potential target for the development of new antimicrobials. RNase P has a high "pharmaceutical index", meaning that it is very highly conserved in Bacteria, so that anything that interferes with one bacterial RNase P is likely to be effective against a wide range of bacterial RNase P's, resulting in a broad-spectrum antimicrobial, and yet very different in eukaryotes, specifically in humans (even the mitochondrion), so that any such compound is unlikely to be cytotoxic. It is a large RNA:protein complex that is essential for life - just like the ribosome, against which a large fraction of natural and synthetic antimicrobials act.