Publication – Göringer

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

C. Voigt, M. Dobrychłop, E. Kruse, A. Czerwoniec, J. M. Kasprzak, P. Bytner, C. Del Campo, W-M. Leeder, J. M. Bujnicki, H. U. Göringer.
Nucleic Acids Research. 2018

Full publication here: The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity

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.