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Nucleic Acids Research Advance Access originally published online on February 3, 2009
Nucleic Acids Research 2009 37(6):1897-1906; doi:10.1093/nar/gkp049
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Nucleic Acids Research, 2009, Vol. 37, No. 6 1897-1906
© 2009 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.

RNA

Kinetoplastid RNA editing involves a 3' nucleotidyl phosphatase activity

Moritz Niemann, Heike Kaibel, Elke Schlüter, Kerstin Weitzel, Michael Brecht and H. Ulrich Göringer*

Genetics, Darmstadt University of Technology, Schnittspahnstraße 10, 64287 Darmstadt, 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 September 23, 2008. Revised January 15, 2009. Accepted January 16, 2009.

Mitochondrial pre-messenger RNAs (pre-mRNAs) in African trypanosomes require RNA editing in order to mature into functional transcripts. The process involves the addition and/or removal of U nucleotides and is mediated by a high-molecular-mass complex, the editosome. Editosomes catalyze the reaction through an enzyme-driven pathway that includes endo/exoribonuclease, terminal uridylate transferase and RNA ligase activities. Here we show that editing involves an additional reaction step, a 3' nucleotidyl phosphatase activity. The activity is associated with the editing complex and we demonstrate that the editosomal proteins TbMP99 and TbMP100 contribute to the activity. Both polypeptides contain endo-exonuclease-phosphatase domains and we show that gene ablation of either one of the two polypeptides is compensated by the other protein. However, simultaneous knockdown of both genes results in trypanosome cells with reduced 3' nucleotidyl phosphatase and reduced editing activity. The data provide a rationale for the exoUase activity of the editosomal protein TbMP42, which generates nonligatable 3' phosphate termini. Opposing phosphates at the two pre-mRNA cleavage fragments likely function as a roadblock to prevent premature ligation.


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