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Nucleic Acids Research, Vol 26, Issue 14 3333-3339, Copyright © 1998 by Oxford University Press

ARTICLES

Comparative structure analysis of vertebrate ribonuclease P RNA

C Pitulle, M Garcia-Paris, KR Zamudio and NR Pace
Departments of Plant & Microbial Biology and Molecular & Cell Biology, University of California, 111 Koshland Hall, #371, Berkeley, CA 94720- 3102, USA.

Ribonuclease P cleaves 5'-precursor sequences from pre-tRNAs. All cellular RNase P holoenzymes contain homologous RNA elements; the eucaryal RNase P RNA, in contrast to the bacterial RNA, is catalytically inactive in the absence of the protein component(s). To understand the function of eucaryal RNase P RNA, knowledge of its structure is needed. Considerable effort has been devoted to comparative studies of the structure of this RNA from diverse organisms, including eucaryotes, primarily fungi, but also a limited set of vertebrates. The substantial differences in the sequences and structures of the vertebrate RNAs from those of other organisms have made it difficult to align the vertebrate sequences, thus limiting comparative studies. To expand our understanding of the structure of diverse RNase P RNAs, we have isolated by PCR and sequenced 13 partial RNase P RNA genes from 11 additional vertebrate taxa representing most extant major vertebrate lineages. Based on a recently proposed structure of the core elements of RNase P RNA, we aligned the sequences and propose a minimum consensus secondary structure for the vertebrate RNase P RNA.
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