Voigt, Christin ; Dobrychlop, Mateusz ; Kruse, Elisabeth ; Czerwoniec, Anna ; Kasprzak, Joanna M. ; Bytner, Patrycja ; Campo, Cristian del ; Leeder, W.-Matthias ; Bujnicki, Janusz M. ; Göringer, H. Ulrich (2018)
The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity.
In: Nucleic acids research, 46 (19)
doi: 10.1093/nar/gky668
Artikel, Bibliographie
Kurzbeschreibung (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.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2018 |
| Autor(en): | Voigt, Christin ; Dobrychlop, Mateusz ; Kruse, Elisabeth ; Czerwoniec, Anna ; Kasprzak, Joanna M. ; Bytner, Patrycja ; Campo, Cristian del ; Leeder, W.-Matthias ; Bujnicki, Janusz M. ; Göringer, H. Ulrich |
| Art des Eintrags: | Bibliographie |
| Titel: | The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity |
| Sprache: | Englisch |
| Publikationsjahr: | 2 November 2018 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Nucleic acids research |
| Jahrgang/Volume einer Zeitschrift: | 46 |
| (Heft-)Nummer: | 19 |
| DOI: | 10.1093/nar/gky668 |
| Kurzbeschreibung (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. |
| ID-Nummer: | pmid:30060205 |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > Genregulation und RNA-Therapeutika |
| Hinterlegungsdatum: | 28 Aug 2018 06:27 |
| Letzte Änderung: | 02 Aug 2021 13:35 |
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