ArticleEukaryotic cell2012
Multifunctional G-rich and RRM-containing domains of TbRGG2 perform separate yet essential functions in trypanosome RNA editing.
Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 22 citations in OpenAlex.
- How Binding Site Flexibility Promotes RNA Scanning by TbRGG2 RRM: A Molecular Dynamics Simulation Study.Journal of chemical information and modeling · 2025Article
- Structural basis of gRNA stabilization and mRNA recognition in trypanosomal RNA editing.Science (New York, N.Y.) · 2023Article
- Structure of the T. brucei kinetoplastid RNA editing substrate-binding complex core component, RESC5.PloS one · 2023Article
- Conserved and transcript-specific functions of the RESC factors, RESC13 and RESC14, in kinetoplastid RNA editing.RNA (New York, N.Y.) · 2022Article
- Lexis and Grammar of Mitochondrial RNA Processing in Trypanosomes.Trends in parasitology · 2020Review
- MRB10130 is a RESC assembly factor that promotes kinetoplastid RNA editing initiation and progression.RNA (New York, N.Y.) · 2019Article
- The RRM of the kRNA-editing protein TbRGG2 uses multiple surfaces to bind and remodel RNA.Nucleic acids research · 2019Article
- Combinatorial interplay of RNA-binding proteins tunes levels of mitochondrial mRNA in trypanosomes.RNA (New York, N.Y.) · 2018Article
- MRB7260 is essential for productive protein-RNA interactions within the RNA editing substrate binding complex during trypanosome RNA editing.RNA (New York, N.Y.) · 2018Article
- Trypanosome RNA Editing Mediator Complex proteins have distinct functions in gRNA utilization.Nucleic acids research · 2017Article
- Article
- High-throughput sequencing of partially edited trypanosome mRNAs reveals barriers to editing progression and evidence for alternative editing.RNA (New York, N.Y.) · 2016Article
- A Protein Complex Map of Trypanosoma brucei.PLoS neglected tropical diseases · 2016Article
- U-Insertion/Deletion mRNA-Editing Holoenzyme: Definition in Sight.Trends in parasitology · 2016Review
- Integrity of the core mitochondrial RNA-binding complex 1 is vital for trypanosome RNA editing.RNA (New York, N.Y.) · 2015Article
- An arginine-glycine-rich RNA binding protein impacts the abundance of specific mRNAs in the mitochondria of Trypanosoma brucei.Eukaryotic cell · 2015Article
- Dual core processing: MRB1 is an emerging kinetoplast RNA editing complex.Trends in parasitology · 2013Review
- A core MRB1 complex component is indispensable for RNA editing in insect and human infective stages of Trypanosoma brucei.PloS one · 2013Article
- Trypanosome RNA editing: the complexity of getting U in and taking U out.Wiley interdisciplinary reviews. RNAReview
- Stunning Intricacies of RNA Editing Complexes RECC, RESC, and REH2C: Functional Organization, Developmental Regulation, and Evolutionary History in Kinetoplastid Protists.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Efficient editing of Trypanosoma brucei mitochondrial RNAs involves the actions of multiple accessory factors. T. brucei RGG2 (TbRGG2) is an essential protein crucial for initiation and 3'-to-5' progression of editing. TbRGG2 comprises an N-terminal G-rich region containing GWG and RG repeats and a C-terminal RNA recognition motif (RRM)-containing domain. Here, we perform in vitro and in vivo separation-of-function studies to interrogate the mechanism of TbRGG2 action in RNA editing. TbRGG2 preferentially binds preedited mRNA in vitro with high affinity attributable to its G-rich region. RNA-annealing and -melting activities are separable, carried out primarily by the G-rich and RRM domains, respectively. In vivo, the G-rich domain partially complements TbRGG2 knockdown, but the RRM domain is also required. Notably, TbRGG2's RNA-melting activity is dispensable for RNA editing in vivo. Interactions between TbRGG2 and MRB1 complex proteins are mediated by both G-rich and RRM-containing domains, depending on the binding partner. Overall, our results are consistent with a model in which the high-affinity RNA binding and RNA-annealing activities of the G-rich domain are essential for RNA editing in vivo. The RRM domain may have key functions involving interactions with the MRB1 complex and/or regulation of the activities of the G-rich domain.
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