RT Journal Article SR Electronic T1 Surface-driven RNA-refolding by the OB-fold proteins of the Trypanosoma brucei editosome JF bioRxiv FD Cold Spring Harbor Laboratory SP 099705 DO 10.1101/099705 A1 Christin Voigt A1 Mateusz Dobrychłop A1 Elisabeth Kruse A1 Anna Czerwoniec A1 Joanna M. Kasprzak A1 Patrycja Bytner A1 Janusz M. Bujnicki A1 H. Ulrich Göringer YR 2017 UL http://biorxiv.org/content/early/2017/01/31/099705.abstract AB RNA editing in African trypanosomes represents an RNA-processing reaction that generates functional mitochondrial transcripts from sequence-deficient pre-mRNAs. The reaction is catalyzed by a macromolecular protein complex known as the editosome. Editosomes have been demonstrated to execute RNA-chaperone activity to overcome the highly folded nature of pre-edited substrate mRNAs. The molecular basis of this activity is unknown. Here we test five OB-fold proteins of the editosome as potential candidates. We show that the different proteins interact by hetero-oligomerization and we demonstrate that all proteins execute RNA-chaperone activity. Activity differences correlate with the surface areas of the proteins and map predominantly to the intrinsically disordered subdomains of the polypeptides. To provide a structural context for our findings we present a coarse-grained model of the editosome. The model suggests that an inner core of catalytically active editosome components is separated from an outer shell of IDP-domains that act as RNA-remodeling sites.