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Nucleic Acids Research Advance Access published online on July 4, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn410
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

TbMP42 is a structure-sensitive ribonuclease that likely follows a metal ion catalysis mechanism

Moritz Niemann1, Michael Brecht1, Elke Schlüter1, Kerstin Weitzel1, Martin Zacharias2 and H. Ulrich Göringer1,*

1Genetics, Darmstadt University of Technology, Schnittspahnstraße 10, 64287 Darmstadt and 2Computational Biology, Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany

*To whom correspondence should be addressed. Tel: +49 6151 16 28 55; Fax: +49 6151-16 56 40; Email: goringer{at}hrzpub.tu-darmstadt.de

Received May 6, 2008. Revised June 10, 2008. Accepted June 10, 2008.

RNA editing in African trypanosomes is characterized by a uridylate-specific insertion and/or deletion reaction that generates functional mitochondrial transcripts. The process is catalyzed by a multi-enzyme complex, the editosome, which consists of approximately 20 proteins. While for some of the polypeptides a contribution to the editing reaction can be deduced from their domain structure, the involvement of other proteins remains elusive. TbMP42, is a component of the editosome that is characterized by two C2H2-type zinc-finger domains and a putative oligosaccharide/oligonucleotide-binding fold. Recombinant TbMP42 has been shown to possess endo/exoribonuclease activity in vitro; however, the protein lacks canonical nuclease motifs. Using a set of synthetic gRNA/pre-mRNA substrate RNAs, we demonstrate that TbMP42 acts as a topology-dependent ribonuclease that is sensitive to base stacking. We further show that the chelation of Zn2+ cations is inhibitory to the enzyme activity and that the chemical modification of amino acids known to coordinate Zn2+ inactivates rTbMP42. Together, the data are suggestive of a Zn2+-dependent metal ion catalysis mechanism for the ribonucleolytic activity of rTbMP42.


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