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Kinetoplastid RNA editing involves a 3' nucleotidyl phosphatase activity.

Niemann, Moritz ; Kaibel, Heike ; Schlüter, Elke ; Weitzel, Kerstin ; Brecht, Michael ; Göringer, H. Ulrich (2009)
Kinetoplastid RNA editing involves a 3' nucleotidyl phosphatase activity.
In: Nucleic acids research, 37 (6)
Artikel, Bibliographie

Kurzbeschreibung (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.

Typ des Eintrags: Artikel
Erschienen: 2009
Autor(en): Niemann, Moritz ; Kaibel, Heike ; Schlüter, Elke ; Weitzel, Kerstin ; Brecht, Michael ; Göringer, H. Ulrich
Art des Eintrags: Bibliographie
Titel: Kinetoplastid RNA editing involves a 3' nucleotidyl phosphatase activity.
Sprache: Englisch
Publikationsjahr: 2009
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Nucleic acids research
Jahrgang/Volume einer Zeitschrift: 37
(Heft-)Nummer: 6
Kurzbeschreibung (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.

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie > Genregulation und RNA-Therapeutika
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10 Fachbereich Biologie
Hinterlegungsdatum: 03 Nov 2011 12:55
Letzte Änderung: 05 Mär 2013 09:55
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