ArticleNucleic acids research2019
The RRM of the kRNA-editing protein TbRGG2 uses multiple surfaces to bind and remodel RNA.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 10 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
- RESC14 and RESC8 cooperate to mediate RESC function and dynamics during trypanosome RNA editing.Nucleic acids research · 2024Article
- Crystal structure of the RNA-recognition motif of Drosophila melanogaster tRNA (uracil-5-)-methyltransferase homolog A.Acta crystallographica. Section F, Structural biology communications · 2024Article
- 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
- The La-related proteins: structures and interactions of a versatile superfamily of RNA-binding proteins.RNA biology · 2021Review
- Comprehensive classification of ABC ATPases and their functional radiation in nucleoprotein dynamics and biological conflict systems.Nucleic acids research · 2020Review
- 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
- Stunning Intricacies of RNA Editing Complexes RECC, RESC, and REH2C: Functional Organization, Developmental Regulation, and Evolutionary History in Kinetoplastid Protists.Wiley interdisciplinary reviews. RNAReview
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7 authors at 1 institution in 1 country.
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Abstract
Kinetoplastid RNA (kRNA) editing takes place in the mitochondria of kinetoplastid protists and creates translatable mRNAs by uridine insertion/deletion. Extensively edited (pan-edited) transcripts contain quadruplex forming guanine stretches, which must be remodeled to promote uridine insertion/deletion. Here we show that the RRM domain of the essential kRNA-editing factor TbRGG2 binds poly(G) and poly(U) RNA and can unfold both. A region C-terminal to the RRM mediates TbRGG2 dimerization, enhancing RNA binding. A RRM-U4 RNA structure reveals a unique RNA-binding mechanism in which the two RRMs of the dimer employ aromatic residues outside the canonical RRM RNA-binding motifs to encase and wrench open the RNA, while backbone atoms specify the uridine bases. Notably, poly(G) RNA is bound via a different binding surface. Thus, these data indicate that TbRGG2 RRM can bind and remodel several RNA substrates suggesting how it might play multiple roles in the kRNA editing process.
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