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

Autor:	Voigt C; Molecular Genetics, Darmstadt University of Technology, Darmstadt, Germany., Dobrychlop M; Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Poznan, Poland., Kruse E; Molecular Genetics, Darmstadt University of Technology, Darmstadt, Germany., Czerwoniec A; Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Poznan, Poland., Kasprzak JM; Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Poznan, Poland., Bytner P; Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Poznan, Poland., Campo CD; Molecular Genetics, Darmstadt University of Technology, Darmstadt, Germany., Leeder WM; Molecular Genetics, Darmstadt University of Technology, Darmstadt, Germany., Bujnicki JM; Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Poznan, Poland.; Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology, Warsaw, Poland., Göringer HU; Molecular Genetics, Darmstadt University of Technology, Darmstadt, Germany.
Jazyk:	angličtina
Zdroj:	Nucleic acids research [Nucleic Acids Res] 2018 Nov 02; Vol. 46 (19), pp. 10353-10367.
DOI:	10.1093/nar/gky668
Abstrakt:	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.
Databáze:	MEDLINE
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