TU Darmstadt / ULB / TUbiblio

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

Voigt, Christin and Dobrychlop, Mateusz and Kruse, Elisabeth and Czerwoniec, Anna and Kasprzak, Joanna M. and Bytner, Patrycja and Campo, Cristian Del and Leeder, W.-Matthias and Bujnicki, Janusz M. and Göringer, H. Ulrich (2018):
The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity.
In: Nucleic acids research, pp. 10353-10367, 46, (19), ISSN 1362-4962,
DOI: 10.1093/nar/gky668,
[Article]

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.

Item Type: Article
Erschienen: 2018
Creators: Voigt, Christin and Dobrychlop, Mateusz and Kruse, Elisabeth and Czerwoniec, Anna and Kasprzak, Joanna M. and Bytner, Patrycja and Campo, Cristian Del and Leeder, W.-Matthias and Bujnicki, Janusz M. and Göringer, H. Ulrich
Title: The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity.
Language: English
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.

Journal or Publication Title: Nucleic acids research
Volume: 46
Number: 19
Divisions: 10 Department of Biology
10 Department of Biology > Postranscriptional Gene Regulation and RNA Therapeutics
Date Deposited: 28 Aug 2018 06:27
DOI: 10.1093/nar/gky668
Identification Number: pmid:30060205
Export:

Optionen (nur für Redakteure)

View Item View Item