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Kinetoplastid RNA editing involves a 3' nucleotidyl phosphatase activity.

Niemann, Moritz and Kaibel, Heike and Schlüter, Elke and Weitzel, Kerstin and Brecht, Michael and Göringer, H. Ulrich (2009):
Kinetoplastid RNA editing involves a 3' nucleotidyl phosphatase activity.
37, In: Nucleic acids research, (6), pp. 1897-906, ISSN 1362-4962, [Article]

Abstract

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.

Item Type: Article
Erschienen: 2009
Creators: Niemann, Moritz and Kaibel, Heike and Schlüter, Elke and Weitzel, Kerstin and Brecht, Michael and Göringer, H. Ulrich
Title: Kinetoplastid RNA editing involves a 3' nucleotidyl phosphatase activity.
Language: English
Abstract:

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.

Journal or Publication Title: Nucleic acids research
Volume: 37
Number: 6
Divisions: 10 Department of Biology > Postranscriptional Gene Regulation and RNA Therapeutics
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10 Department of Biology
Date Deposited: 03 Nov 2011 12:55
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