The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity

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Abstract

Sequence-deficient mitochondrial pre-mRNAs in African trypanosomes are substrates of a Unucleotide- 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 preedited 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 coarsegrained 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.

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APA

Voigt, C., Dobrych-Lop, M., Kruse, E., Czerwoniec, A., Kasprzak, J. M., Bytner, P., … Göringer, H. U. (2018). The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity. Nucleic Acids Research, 46(19), 10353–10367. https://doi.org/10.1093/nar/gky668

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