Brecht, Michael ; Niemann, Moritz ; Schlüter, Elke ; Müller, Ulrich F. ; Stuart, Ken ; Göringer, H. Ulrich (2005)
TbMP42, a protein component of the RNA editing complex in African trypanosomes, has endo-exoribonuclease activity.
In: Molecular cell, 17 (5)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
RNA editing in trypanosomatids is catalyzed by a high molecular mass RNP complex, which is only partially characterized. TbMP42 is a 42 kDa protein of unknown function that copurifies with the editing complex. The polypeptide is characterized by two Zn fingers and a potential barrel structure/OB-fold at its C terminus. Using recombinant TbMP42, we show that the protein can bind to dsRNA and dsDNA but fails to recognize DNA/RNA hybrids. rTbMP42 degrades ssRNA by a 3' to 5' exoribonuclease activity. In addition, rTbMP42 has endoribonuclease activity, which preferentially hydrolyzes non-base-paired uridylate-containing sequences. Gene silencing of TbMP42 inhibits cell growth and is ultimately lethal to the parasite. Mitochondrial extracts from TbMP42-minus trypanosomes have only residual RNA editing activity and strongly reduced endo-exoribonuclease activity. However, all three activities can be restored by the addition of rTbMP42. Together, the data suggest that TbMP42 contributes both endo- and exoribonuclease activity to the editing reaction cycle.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2005 |
| Autor(en): | Brecht, Michael ; Niemann, Moritz ; Schlüter, Elke ; Müller, Ulrich F. ; Stuart, Ken ; Göringer, H. Ulrich |
| Art des Eintrags: | Bibliographie |
| Titel: | TbMP42, a protein component of the RNA editing complex in African trypanosomes, has endo-exoribonuclease activity. |
| Sprache: | Englisch |
| Publikationsjahr: | 2005 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Molecular cell |
| Jahrgang/Volume einer Zeitschrift: | 17 |
| (Heft-)Nummer: | 5 |
| Kurzbeschreibung (Abstract): | RNA editing in trypanosomatids is catalyzed by a high molecular mass RNP complex, which is only partially characterized. TbMP42 is a 42 kDa protein of unknown function that copurifies with the editing complex. The polypeptide is characterized by two Zn fingers and a potential barrel structure/OB-fold at its C terminus. Using recombinant TbMP42, we show that the protein can bind to dsRNA and dsDNA but fails to recognize DNA/RNA hybrids. rTbMP42 degrades ssRNA by a 3' to 5' exoribonuclease activity. In addition, rTbMP42 has endoribonuclease activity, which preferentially hydrolyzes non-base-paired uridylate-containing sequences. Gene silencing of TbMP42 inhibits cell growth and is ultimately lethal to the parasite. Mitochondrial extracts from TbMP42-minus trypanosomes have only residual RNA editing activity and strongly reduced endo-exoribonuclease activity. However, all three activities can be restored by the addition of rTbMP42. Together, the data suggest that TbMP42 contributes both endo- and exoribonuclease activity to the editing reaction cycle. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie > Genregulation und RNA-Therapeutika ?? fb10_mikrobiologie ?? 10 Fachbereich Biologie |
| Hinterlegungsdatum: | 03 Nov 2011 13:07 |
| Letzte Änderung: | 05 Mär 2013 09:55 |
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