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TbMP42 is a structure-sensitive ribonuclease that likely follows a metal ion catalysis mechanism.

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
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10 Fachbereich Biologie
Hinterlegungsdatum: 03 Nov 2011 12:56
Letzte Änderung: 05 Mär 2013 09:55
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