ArticleMolecular and cellular biology2007
In Trypanosoma brucei RNA editing, TbMP18 (band VII) is critical for editosome integrity and for both insertional and deletional cleavages.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 22 citations in OpenAlex.
- Omics data integration facilitates target selection for new antiparasitic drugs against TriTryp infections.Frontiers in pharmacology · 2023Article
- Lexis and Grammar of Mitochondrial RNA Processing in Trypanosomes.Trends in parasitology · 2020Review
- The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity.Nucleic acids research · 2018Article
- The Architecture of Trypanosoma brucei editosomes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Explorations of linked editosome domains leading to the discovery of motifs defining conserved pockets in editosome OB-folds.Journal of structural biology · 2012Article
- The structure of the C-terminal domain of the largest editosome interaction protein and its role in promoting RNA binding by RNA-editing ligase L2.Nucleic acids research · 2012Article
- Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody.Nucleic acids research · 2012Article
- Structures of a key interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies.Journal of structural biology · 2011Article
- A protein-protein interaction map of trypanosome ~20S editosomes.The Journal of biological chemistry · 2010Article
- The zinc-fingers of KREPA3 are essential for the complete editing of mitochondrial mRNAs in Trypanosoma brucei.PloS one · 2010Article
- Article
- The KREPA3 zinc finger motifs and OB-fold domain are essential for RNA editing and survival of Trypanosoma brucei.Molecular and cellular biology · 2008Article
- Guide RNA-binding complex from mitochondria of trypanosomatids.Molecular cell · 2008Article
- Trypanosoma brucei RNA editing protein TbMP42 (band VI) is crucial for the endonucleolytic cleavages but not the subsequent steps of U-deletion and U-insertion.RNA (New York, N.Y.) · 2008Article
- Trypanosoma brucei RNA editing: coupled cycles of U deletion reveal processive activity of the editing complex.Molecular and cellular biology · 2008Article
- KREPA6 is an RNA-binding protein essential for editosome integrity and survival of Trypanosoma brucei.RNA (New York, N.Y.) · 2008Article
- Stunning Intricacies of RNA Editing Complexes RECC, RESC, and REH2C: Functional Organization, Developmental Regulation, and Evolutionary History in Kinetoplastid Protists.Wiley interdisciplinary reviews. RNAReview
- Uridine insertion/deletion editing in trypanosomes: a playground for RNA-guided information transfer.Wiley interdisciplinary reviews. RNAReview
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3 authors at 1 institution in 1 country.
Funding
Abstract
In trypanosome RNA editing, uridylate (U) residues are inserted and deleted at numerous sites within mitochondrial pre-mRNAs by an approximately 20S protein complex that catalyzes cycles of cleavage, U addition/U removal, and ligation. We used RNA interference to deplete TbMP18 (band VII), the last unexamined major protein of our purified editing complex, showing it is essential. TbMP18 is critical for the U-deletional and U-insertional cleavages and for integrity of the approximately 20S editing complex, whose other major components, TbMP99, TbMP81, TbMP63, TbMP52, TbMP48, TbMP42 (bands I through VI), and TbMP57, instead sediment as approximately 10S associations. Additionally, TbMP18 augments editing substrate recognition by the TbMP57 terminal U transferase, possibly aiding the recognition component, TbMP81. The other editing activities and their coordination in precleaved editing remain active in the absence of TbMP18. These data are reminiscent of the data on editing subcomplexes reported by A. Schnaufer et al. (Mol. Cell 12:307-319, 2003) and suggest that these subcomplexes are held together in the approximately 20S complex by TbMP18, as was proposed previously. Our data additionally imply that the proteins are less long-lived in these subcomplexes than they are when held in the complete editing complex. The editing endonucleolytic cleavages being lost when the editing complex becomes fragmented, as upon TbMP18 depletion, should be advantageous to the trypanosome, minimizing broken mRNAs.
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