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Nucleic Acids Res. 2018 Nov 2;46(19):10353-10367. doi: 10.1093/nar/gky668.

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

Author information

1
Molecular Genetics, Darmstadt University of Technology, Darmstadt, Germany.
2
Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Poznan, Poland.
3
Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology, Warsaw, Poland.

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.

PMID:
30060205
PMCID:
PMC6212840
DOI:
10.1093/nar/gky668
[Indexed for MEDLINE]
Free PMC Article

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