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Nucleic Acids Research 2005 33(21):6920-6930; doi:10.1093/nar/gki993
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Published online 6 December 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

The naturally trans-acting ribozyme RNase P RNA has leadzyme properties

Ema Kikovska, Nils-Egil Mikkelsen1 and Leif A. Kirsebom*

Department of Cell and Molecular Biology, Uppsala University Box 596, Biomedical Centre, SE-751 24 Uppsala, Sweden 1Department of Molecular Biology, Swedish Agricultural University Box 590, Biomedical Centre, SE-751 23 Uppsala, Sweden

*To whom correspondence should be addressed. Tel: +46 18 471 4068; Fax: +46 18 53 03 96; Email: Leif.Kirsebom{at}icm.uu.se

Received June 7, 2005. Revised August 30, 2005. Accepted November 16, 2005.

Divalent metal ions promote hydrolysis of RNA backbones generating 5'OH and 2';3'P as cleavage products. In these reactions, the neighboring 2'OH act as the nucleophile. RNA catalyzed reactions also require divalent metal ions and a number of different metal ions function in RNA mediated cleavage of RNA. In one case, the LZV leadzyme, it was shown that this catalytic RNA requires lead for catalysis. So far, none of the naturally isolated ribozymes have been demonstrated to use lead to activate the nucleophile. Here we provide evidence that RNase P RNA, a naturally trans-acting ribozyme, has leadzyme properties. But, in contrast to LZV RNA, RNase P RNA mediated cleavage promoted by Pb2+ results in 5' phosphate and 3'OH as cleavage products. Based on our findings, we infer that Pb2+ activates H2O to act as the nucleophile and we identified residues both in the substrate and RNase P RNA that most likely influenced the positioning of Pb2+ at the cleavage site. Our data suggest that Pb2+ can promote cleavage of RNA by activating either an inner sphere H2O or a neighboring 2'OH to act as nucleophile.


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Home page
 Proc. Natl. Acad. Sci. USAHome page
E. Kikovska, S. G. Svard, and L. A. Kirsebom
From the Cover: Eukaryotic RNase P RNA mediates cleavage in the absence of protein
PNAS, February 13, 2007; 104(7): 2062 - 2067.
[Abstract] [Full Text] [PDF]


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