Structure and intrinsic disorder of the proteins of theTrypanosoma brucei editosome

• Published in: FEBS letters Vol. 589; no. 19PartA; pp. 2603 - 2610
• Main Authors: Czerwoniec, Anna, Kasprzak, Joanna M., Bytner, Patrycja, Dobrychłop, Mateusz, Bujnicki, Janusz M.
• Format: Journal Article
• Language: English
• Published: 14-09-2015
• Subjects: ASF1 like histone chaperone domain; ASF_hist_chap; C-terminal domain; CTD; double-stranded RNA binding motif; dsRBM; Editosome; Endo/Exo/Phos; endonuclease–exonuclease–phosphatase family motif; GDT_TS; global distance test total score; gRNA; guide RNAs; IDRs; Intrinsic disorder; intrinsically disordered regions; Model Quality Assessment Programs; MQAPs; N-terminal domain; NMR; NTD; Nuclear Magnetic Resonance; nucleotidyltransferase; OB-fold; oligonucleotide/oligosaccharide binding fold; PAP_CTD; PDB; poly(a) polymerase C-terminal domain; PROQ; Protein Data Bank; Protein Quality Predictor; Protein Structure Prediction; Protein–RNA binding; RECC; RMSD; RNA editing; RNA editing core complex; root-mean-square deviation; SANS; SAXS; SCOP; small-angle neutron scattering; small-angle X-ray scattering; Structural Classification of Proteins; TEM; Transmission Electron Microscopy; zinc finger; Znf
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2015.07.026

Mitochondrial pre‐mRNAs in trypanosomatids undergo RNA editing to be converted into translatable mRNAs. The reaction is characterized by the insertion and deletion of uridine residues and is catalyzed by a macromolecular protein complex called the editosome. Despite intensive research, structural information for the majority of editosome proteins is still missing and no high resolution structure for the editosome exists. Here we present a comprehensive structural bioinformatics analysis of all proteins of theTrypanosoma brucei editosome. We specifically focus on the interplay between intrinsic order and disorder. According to computational predictions, editosome proteins involved in the basal reaction steps of the processing cycle are mostly ordered. By contrast, thirty percent of the amino acid content of the editosome is intrinsically disordered, which includes most prominently proteins with OB‐fold domains. Based on the data we suggest a functional model, in which the structurally disordered domains of the complex are correlated with the RNA binding and RNA unfolding activity of theT. brucei editosome.
We predicted intrinsically disordered regions inT. brucei editosome proteins.
We constructed structural models of editosome proteins.
We identified about 30% of the editosome as intrinsically disordered.