ArticleThe Journal of biological chemistry2012
Trypanosoma brucei 20 S editosomes have one RNA substrate-binding site and execute RNA unwinding activity.
Article in The Journal of biological chemistry, 2012. 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, 16 citations in OpenAlex.
- Article
- Mapping the RNA Chaperone Activity of the Trypanosoma brucei Editosome Using SHAPE-Chemical Probing.Methods in molecular biology (Clifton, N.J.) · 2026Article
- KREH1 RNA helicase activity promotes utilization of initiator gRNAs across multiple mRNAs in trypanosome RNA editing.Nucleic acids research · 2023Article
- Fuzzy RNA recognition by the Trypanosoma brucei editosome.Nucleic acids research · 2022Article
- Trypanosomatid, fluorescence-basedBio-protocol · 2021Article
- Analyzing editosome function in high-throughput.Nucleic acids research · 2020Article
- The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity.Nucleic acids research · 2018Article
- The RNA chaperone activity of the Trypanosoma brucei editosome raises the dynamic of bound pre-mRNAs.Scientific reports · 2016Article
- In vivo analysis of trypanosome mitochondrial RNA function by artificial site-specific RNA endonuclease-mediated knockdown.RNA (New York, N.Y.) · 2015Article
- Charge reduction and thermodynamic stabilization of substrate RNAs inhibit RNA editing.PloS one · 2015Article
- Molecular crowding inhibits U-insertion/deletion RNA editing in vitro: consequences for the in vivo reaction.PloS one · 2013Article
- Multifunctional G-rich and RRM-containing domains of TbRGG2 perform separate yet essential functions in trypanosome RNA editing.Eukaryotic cell · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Editing of mitochondrial pre-mRNAs in African trypanosomes generates full-length transcripts by the site-specific insertion and deletion of uridylate nucleotides. The reaction is catalyzed by a 0.8 MDa multienzyme complex, the editosome. Although the binding of substrate pre-edited mRNAs and cognate guide RNAs (gRNAs) represents the first step in the reaction cycle, the biochemical and biophysical details of the editosome/RNA interaction are not understood. Here we show that editosomes bind full-length substrate mRNAs with nanomolar affinity in a nonselective fashion. The complexes do not discriminate-neither kinetically nor thermodynamically-between different mitochondrial pre-mRNAs or between edited and unedited versions of the same transcript. They also bind gRNAs and gRNA/pre-mRNA hybrid RNAs with similar affinities and association rate constants. Gold labeling of editosome-bound RNA in combination with transmission electron microscopy identified a single RNA-binding site per editosome. However, atomic force microscopy of individual pre-mRNA-editosome complexes revealed that multiple editosomes can interact with one pre-mRNA. Lastly, we demonstrate a so far unknown activity of the editing machinery: editosome-bound RNA becomes unfolded by a chaperone-type RNA unwinding activity.
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