ArticleNucleic acids research2009
Kinetoplastid RNA editing involves a 3' nucleotidyl phosphatase activity.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Structural basis for guide RNA trimming by RNase D ribonuclease in Trypanosoma brucei.Nucleic acids research · 2021Article
- Differential Editosome Protein Function between Life Cycle Stages of Trypanosoma brucei.The Journal of biological chemistry · 2015Article
- Trans-splicing and RNA editing of LSU rRNA in Diplonema mitochondria.Nucleic acids research · 2014Article
- RNA-level unscrambling of fragmented genes in Diplonema mitochondria.RNA biology · 2013Article
- Trypanosoma brucei 20 S editosomes have one RNA substrate-binding site and execute RNA unwinding activity.The Journal of biological chemistry · 2012Article
- Editosome accessory factors KREPB9 and KREPB10 in Trypanosoma brucei.Eukaryotic cell · 2012Article
- Article
- A novel member of the RNase D exoribonuclease family functions in mitochondrial guide RNA metabolism in Trypanosoma brucei.The Journal of biological chemistry · 2011Article
- When you can't trust the DNA: RNA editing changes transcript sequences.Cellular and molecular life sciences : CMLS · 2011Review
- Uridine insertion/deletion editing in trypanosomes: a playground for RNA-guided information transfer.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Mitochondrial pre-messenger RNAs (pre-mRNAs) in African trypanosomes require RNA editing in order to mature into functional transcripts. The process involves the addition and/or removal of U nucleotides and is mediated by a high-molecular-mass complex, the editosome. Editosomes catalyze the reaction through an enzyme-driven pathway that includes endo/exoribonuclease, terminal uridylate transferase and RNA ligase activities. Here we show that editing involves an additional reaction step, a 3' nucleotidyl phosphatase activity. The activity is associated with the editing complex and we demonstrate that the editosomal proteins TbMP99 and TbMP100 contribute to the activity. Both polypeptides contain endo-exonuclease-phosphatase domains and we show that gene ablation of either one of the two polypeptides is compensated by the other protein. However, simultaneous knockdown of both genes results in trypanosome cells with reduced 3' nucleotidyl phosphatase and reduced editing activity. The data provide a rationale for the exoUase activity of the editosomal protein TbMP42, which generates nonligatable 3' phosphate termini. Opposing phosphates at the two pre-mRNA cleavage fragments likely function as a roadblock to prevent premature ligation.
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Registered trials
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