ArticleNucleic acids research2008
TbMP42 is a structure-sensitive ribonuclease that likely follows a metal ion catalysis mechanism.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Effect of Divalent Metal Ions on the Ribonuclease Activity of the Toxin Molecule HP0894 fromLife (Basel, Switzerland) · 2024Article
- The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity.Nucleic acids research · 2018Article
- Differential Editosome Protein Function between Life Cycle Stages of Trypanosoma brucei.The Journal of biological chemistry · 2015Article
- Charge reduction and thermodynamic stabilization of substrate RNAs inhibit RNA editing.PloS one · 2015Article
- Trypanosoma brucei 20 S editosomes have one RNA substrate-binding site and execute RNA unwinding activity.The Journal of biological chemistry · 2012Article
- Article
- Naphthalene-based RNA editing inhibitor blocks RNA editing activities and editosome assembly in Trypanosoma brucei.The Journal of biological chemistry · 2011Article
- Characterization of EndoTT, a novel single-stranded DNA-specific endonuclease from Thermoanaerobacter tengcongensis.Nucleic acids research · 2010Article
- Kinetoplastid RNA editing involves a 3' nucleotidyl phosphatase activity.Nucleic acids research · 2009Article
- Snapshots of the RNA editing machine in trypanosomes captured at different assembly stages in vivo.The EMBO journal · 2009Article
- The KREPA3 zinc finger motifs and OB-fold domain are essential for RNA editing and survival of Trypanosoma brucei.Molecular and cellular biology · 2008Article
- Uridine insertion/deletion editing in trypanosomes: a playground for RNA-guided information transfer.Wiley interdisciplinary reviews. RNAReview
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6 authors.
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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.
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