Transfer tRNA in most organisms is transcribed as a precursor with additional sequences at both the 5' and 3' ends. Maturation of the 5' end of tRNA is catalyzed by ribonuclease P (RNase P) across all domains of life, and, until recently, all known RNase P enzymes include a catalytic RNA component.  Bacterial RNase P is composed of a large, catalytic RNA moiety and a small protein cofactor important for molecular recognition.  This enzyme is activated by magnesium ions bound to the RNA subunit.  We are investigating the function and location of catalytic metal ions using single atom mutagenesis.  RNase P from human mitochondria and Arabidopsis thaliana chloroplast and mitochondria are proteinaceous and represent a new class of metallonucleases (PROteinacous RNase P (PRORP)).  We are investigating the structure, function, specificity and metal-dependent mechanism of this novel nuclease.  This work is supported by NIH grant GM055387.

Enzymology of precursor-tRNA processing

244th National Meeting (2012)

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