ArticleRNA (New York, N.Y.)2008
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.
Article in RNA (New York, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 18 citations in OpenAlex.
- Multiple domains of the integral KREPA3 protein are critical for the structure and precise functions of RNA editing catalytic complexes inRNA (New York, N.Y.) · 2023Article
- Multiple domains of the integral KREPA3 protein are critical for the structure and precise functions of RNA Editing Catalytic Complexes inbioRxiv : the preprint server for biology · 2023Article
- Dynamic RNA holo-editosomes with subcomplex variants: Insights into the control of trypanosome editing.Wiley interdisciplinary reviews. RNA · 2018Review
- The Architecture of Trypanosoma brucei editosomes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Differential Editosome Protein Function between Life Cycle Stages of Trypanosoma brucei.The Journal of biological chemistry · 2015Article
- Inhibitors of RNA editing as potential chemotherapeutics against trypanosomatid pathogens.International journal for parasitology. Drugs and drug resistance · 2012Review
- Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody.Nucleic acids research · 2012Article
- Article
- Endonuclease associations with three distinct editosomes in Trypanosoma brucei.The Journal of biological chemistry · 2011Article
- Naphthalene-based RNA editing inhibitor blocks RNA editing activities and editosome assembly in Trypanosoma brucei.The Journal of biological chemistry · 2011Article
- Structures of a key interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies.Journal of structural biology · 2011Article
- A fluorescence-based reporter substrate for monitoring RNA editing in trypanosomatid pathogens.Nucleic acids research · 2010Article
- 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
- Kinetoplastid RNA editing involves a 3' nucleotidyl phosphatase activity.Nucleic acids research · 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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3 authors at 1 institution in 1 country.
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Abstract
Trypanosome mitochondrial mRNAs achieve their coding sequences through RNA editing. This process, catalyzed by approximately 20S protein complexes, involves large numbers of uridylate (U) insertions and deletions within mRNA precursors. Here we analyze the role of the essential TbMP42 protein (band VI/KREPA2) by individually examining each step of the U-deletional and U-insertional editing cycles, using reactions in the approximately linear range. We examined control extracts and RNA interference (RNAi) extracts prepared soon after TbMP42 was depleted (when primary effects should be most evident) and three days later (when precedent shows secondary effects can become prominent). This analysis shows TbMP42 is critical for cleavage of editing substrates by both the U-deletional and U-insertional endonucleases. However, on simple substrates that assess cleavage independent of editing features, TbMP42 is similarly required only for the U-deletional endonuclease, indicating TbMP42 affects the two editing endonucleases differently. Supplementing RNAi extract with recombinant TbMP42 partly restores these cleavage activities. Notably, we find that all the other editing steps (the 3'-U-exonuclease [3'-U-exo] and ligation steps of U-deletion and the terminal-U-transferase [TUTase] and ligation steps of U-insertion) remain at control levels upon RNAi induction, and hence are not dependent on TbMP42. This contrasts with an earlier report that TbMP42 is a 3'-U-exo that may act in U-deletion and additionally is critical for the TUTase and/or ligation steps of U-insertion, observations our data suggest reflect indirect effects of TbMP42 depletion. Thus, trypanosomes require TbMP42 for both endonucleolytic cleavage steps of RNA editing, but not for any of the subsequent steps of the editing cycles.
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