Niemann, Moritz ; Brecht, Michael ; Schlüter, Elke ; Weitzel, Kerstin ; Zacharias, Martin ; Göringer, H. Ulrich (2008)
TbMP42 is a structure-sensitive ribonuclease that likely follows a metal ion catalysis mechanism.
In: Nucleic acids research, 36 (13)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
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 C(2)H(2)-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 Zn(2+) cations is inhibitory to the enzyme activity and that the chemical modification of amino acids known to coordinate Zn(2+) inactivates rTbMP42. Together, the data are suggestive of a Zn(2+)-dependent metal ion catalysis mechanism for the ribonucleolytic activity of rTbMP42.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2008 |
| Autor(en): | Niemann, Moritz ; Brecht, Michael ; Schlüter, Elke ; Weitzel, Kerstin ; Zacharias, Martin ; Göringer, H. Ulrich |
| Art des Eintrags: | Bibliographie |
| Titel: | TbMP42 is a structure-sensitive ribonuclease that likely follows a metal ion catalysis mechanism. |
| Sprache: | Englisch |
| Publikationsjahr: | 2008 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Nucleic acids research |
| Jahrgang/Volume einer Zeitschrift: | 36 |
| (Heft-)Nummer: | 13 |
| Kurzbeschreibung (Abstract): | 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 C(2)H(2)-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 Zn(2+) cations is inhibitory to the enzyme activity and that the chemical modification of amino acids known to coordinate Zn(2+) inactivates rTbMP42. Together, the data are suggestive of a Zn(2+)-dependent metal ion catalysis mechanism for the ribonucleolytic activity of rTbMP42. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie > Genregulation und RNA-Therapeutika ?? fb10_mikrobiologie ?? 10 Fachbereich Biologie |
| Hinterlegungsdatum: | 03 Nov 2011 12:56 |
| Letzte Änderung: | 05 Mär 2013 09:55 |
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