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- W2884698972 abstract "Sequence-deficient mitochondrial pre-mRNAs in African trypanosomes are substrates of a U-nucleotide-specific RNA editing reaction to generate translation-competent mRNAs. The reaction is catalyzed by a macromolecular protein complex termed the editosome. Editosomes execute RNA-chaperone activity to overcome the highly folded nature of pre-edited substrate mRNAs. The molecular basis for this activity is unknown. Here we test five of the OB-fold proteins of the Trypanosoma brucei editosome as candidates. We demonstrate that all proteins execute RNA-chaperone activity albeit to different degrees. We further show that the activities correlate to the surface areas of the proteins and we map the protein-induced RNA-structure changes using SHAPE-chemical probing. To provide a structural context for our findings we calculate a coarse-grained model of the editosome. The model has a shell-like structure: Structurally well-defined protein domains are separated from an outer shell of intrinsically disordered protein domains, which suggests a surface-driven mechanism for the chaperone activity." @default.
- W2884698972 created "2018-08-03" @default.
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- W2884698972 date "2018-07-28" @default.
- W2884698972 modified "2023-10-10" @default.
- W2884698972 title "The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity" @default.
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- W2884698972 doi "https://doi.org/10.1093/nar/gky668" @default.
- W2884698972 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6212840" @default.
- W2884698972 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30060205" @default.
- W2884698972 hasPublicationYear "2018" @default.
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